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Conserved domains on  [gi|564332436|ref|XP_006230941|]
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serine/threonine-protein kinase MARK2 isoform X1 [Rattus norvegicus]

Protein Classification

serine/threonine-protein kinase MARK2( domain architecture ID 10197351)

serine/threonine-protein kinase MARK2 (MAP/microtubule affinity-regulating kinase 2) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is involved in cell polarity and microtubule dynamics regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
52-304 0e+00

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: 594.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14072   81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSK 291
Cdd:cd14072  161 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSK 240
                        250
                 ....*....|...
gi 564332436 292 RGTLEQIMKDRWM 304
Cdd:cd14072  241 RGTLEQIMKDRWM 253
MARK2_C cd12201
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
742-840 1.16e-69

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 2; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK2, also called Par-1b or ELKL motif kinase 1 (EMK-1), is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. It also regulates axon formation and has been implicated in neurodegeneration. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


:

Pssm-ID: 213386  Cd Length: 99  Bit Score: 224.54  E-value: 1.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 742 KPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRI 821
Cdd:cd12201    1 KPRSLRFTWSMKTTSSMEPNEMMKEIRKVLDANNCQYELQEKYMLLCMHGTPGHDDFVQWEMEVCKLPRLSLNGVRFKRI 80
                         90
                 ....*....|....*....
gi 564332436 822 SGTSMAFKNIASKIANELK 840
Cdd:cd12201   81 SGTSIAFKNIASKIANELK 99
UBA_MARK2 cd14406
UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins; MARK2, also ...
322-363 1.71e-23

UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins; MARK2, also called ELKL motif kinase 1 (EMK-1), MAP/microtubule affinity-regulating kinase 2, PAR1 homolog, or PAR1 homolog b (Par-1b), is enriched in brain. It belongs to the AMPK family of Ser/Thr kinases. MARK2 has been implicated in regulating fertility, immune homeostasis, learning, and memory as well as adiposity, insulin hypersensitivity, and glucose metabolism. The activity of MARK2 is necessary for the outgrowth of cell processes, neurites, and dendritic spines. It is a TORC2 (also known as Crtc2) Ser-275 kinase that blocks TORC2-induced cAMP response element binding protein (CREB) activity. It regulates axon formation via phosphorylation of a kinesin-like motor protein GAKIN/KIF13B. It also acts as a positive regulator of Wnt-beta-catenin signaling.


:

Pssm-ID: 270589  Cd Length: 42  Bit Score: 93.52  E-value: 1.71e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 564332436 322 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 363
Cdd:cd14406    1 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 42
 
Name Accession Description Interval E-value
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
52-304 0e+00

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: 594.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14072   81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSK 291
Cdd:cd14072  161 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSK 240
                        250
                 ....*....|...
gi 564332436 292 RGTLEQIMKDRWM 304
Cdd:cd14072  241 RGTLEQIMKDRWM 253
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
53-304 6.98e-112

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 341.82  E-value: 6.98e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436    53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI-KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   213 PPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDG-QNLKELRERVLRGKYRIPFYM---STDCENLLKKFLILN 288
Cdd:smart00220 160 PEYMAPEVLLGKGYGKA-VDIWSLGVILYELLTGKPPFPGdDQLLELFKKIGKPKPPFPPPEwdiSPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 564332436   289 PSKRGTLEQIMKDRWM 304
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
53-304 4.59e-70

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 230.21  E-value: 4.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVqychqkfivhrdlkaENllldadmnikiadfgfsneftfGNKLDTFCGS 212
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL---------------ES----------------------GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  213 PPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PFYMSTDCENLLKKFLILNP 289
Cdd:pfam00069 124 PWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFpelPSNLSEEAKDLLKKLLKKDP 202
                         250
                  ....*....|....*
gi 564332436  290 SKRGTLEQIMKDRWM 304
Cdd:pfam00069 203 SKRLTATQALQHPWF 217
MARK2_C cd12201
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
742-840 1.16e-69

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 2; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK2, also called Par-1b or ELKL motif kinase 1 (EMK-1), is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. It also regulates axon formation and has been implicated in neurodegeneration. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213386  Cd Length: 99  Bit Score: 224.54  E-value: 1.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 742 KPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRI 821
Cdd:cd12201    1 KPRSLRFTWSMKTTSSMEPNEMMKEIRKVLDANNCQYELQEKYMLLCMHGTPGHDDFVQWEMEVCKLPRLSLNGVRFKRI 80
                         90
                 ....*....|....*....
gi 564332436 822 SGTSMAFKNIASKIANELK 840
Cdd:cd12201   81 SGTSIAFKNIASKIANELK 99
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
50-292 2.48e-64

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 223.74  E-value: 2.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFrREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN--KL 206
Cdd:COG0515   86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATltQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDC----ENLLK 282
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVD-PRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLppalDAIVL 244
                        250
                 ....*....|
gi 564332436 283 KFLILNPSKR 292
Cdd:COG0515  245 RALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
52-301 2.20e-53

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 188.49  E-value: 2.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKLDTFC 210
Cdd:PTZ00263  99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP--DRTFTLC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:PTZ00263 177 GTPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHT 255
                        250
                 ....*....|..
gi 564332436 291 KR-GTLEQIMKD 301
Cdd:PTZ00263 256 KRlGTLKGGVAD 267
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
51-262 3.95e-37

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 147.63  E-value: 3.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQL-NSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:NF033483   7 GRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL-RPDLaRDPEFVARFrREAQSAASLSHPNIVSVYDVGEDGGIPYIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNE-FTFG 203
Cdd:NF033483  86 MEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTtMTQT 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 204 NKLdtfCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-----LKELRERV 262
Cdd:NF033483 166 NSV---LGTVHYLSPEQARGGTVD-ARSDIYSLGIVLYEMLTGRPPFDGDSpvsvaYKHVQEDP 225
UBA_MARK2 cd14406
UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins; MARK2, also ...
322-363 1.71e-23

UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins; MARK2, also called ELKL motif kinase 1 (EMK-1), MAP/microtubule affinity-regulating kinase 2, PAR1 homolog, or PAR1 homolog b (Par-1b), is enriched in brain. It belongs to the AMPK family of Ser/Thr kinases. MARK2 has been implicated in regulating fertility, immune homeostasis, learning, and memory as well as adiposity, insulin hypersensitivity, and glucose metabolism. The activity of MARK2 is necessary for the outgrowth of cell processes, neurites, and dendritic spines. It is a TORC2 (also known as Crtc2) Ser-275 kinase that blocks TORC2-induced cAMP response element binding protein (CREB) activity. It regulates axon formation via phosphorylation of a kinesin-like motor protein GAKIN/KIF13B. It also acts as a positive regulator of Wnt-beta-catenin signaling.


Pssm-ID: 270589  Cd Length: 42  Bit Score: 93.52  E-value: 1.71e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 564332436 322 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 363
Cdd:cd14406    1 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 42
KA1 pfam02149
Kinase associated domain 1;
799-841 1.38e-18

Kinase associated domain 1;


Pssm-ID: 460465  Cd Length: 44  Bit Score: 79.82  E-value: 1.38e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564332436  799 VQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL 841
Cdd:pfam02149   2 VKFEIEVCKLPRLSLYGVDFKRLSGDTWQYKDLASKILSELRL 44
 
Name Accession Description Interval E-value
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
52-304 0e+00

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: 594.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14072   81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSK 291
Cdd:cd14072  161 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSK 240
                        250
                 ....*....|...
gi 564332436 292 RGTLEQIMKDRWM 304
Cdd:cd14072  241 RGTLEQIMKDRWM 253
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
53-304 1.61e-160

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: 467.25  E-value: 1.61e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:cd14071   82 SNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd14071  162 PPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSKR 241
                        250
                 ....*....|..
gi 564332436 293 GTLEQIMKDRWM 304
Cdd:cd14071  242 LTIEQIKKHKWM 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
52-303 1.27e-158

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: 462.37  E-value: 1.27e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14003   81 ASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSK 291
Cdd:cd14003  161 TPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSK 240
                        250
                 ....*....|..
gi 564332436 292 RGTLEQIMKDRW 303
Cdd:cd14003  241 RITIEEILNHPW 252
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
50-304 1.56e-123

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: 371.99  E-value: 1.56e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQ-KLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14079    1 IGNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEeKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14079   81 MEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14079  161 SCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVD 240
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14079  241 PLKRITIPEIRQHPWF 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
51-304 1.59e-118

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: 359.26  E-value: 1.59e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd14081    1 GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLsKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14081   81 EYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLETS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNP 289
Cdd:cd14081  161 CGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNP 240
                        250
                 ....*....|....*
gi 564332436 290 SKRGTLEQIMKDRWM 304
Cdd:cd14081  241 EKRITIEEIKKHPWF 255
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
52-303 1.71e-114

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: 348.70  E-value: 1.71e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd05117   81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGEKLKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYM----STDCENLLKKF 284
Cdd:cd05117  161 VCGTPYYVAPEVLKGKGY-GKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEwknvSEEAKDLIKRL 239
                        250
                 ....*....|....*....
gi 564332436 285 LILNPSKRGTLEQIMKDRW 303
Cdd:cd05117  240 LVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
53-304 6.98e-112

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 341.82  E-value: 6.98e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436    53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI-KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   213 PPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDG-QNLKELRERVLRGKYRIPFYM---STDCENLLKKFLILN 288
Cdd:smart00220 160 PEYMAPEVLLGKGYGKA-VDIWSLGVILYELLTGKPPFPGdDQLLELFKKIGKPKPPFPPPEwdiSPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 564332436   289 PSKRGTLEQIMKDRWM 304
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
50-304 1.16e-109

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: 336.23  E-value: 1.16e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd14075    1 IGFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14075   81 EYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNP 289
Cdd:cd14075  161 CGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVP 240
                        250
                 ....*....|....*
gi 564332436 290 SKRGTLEQIMKDRWM 304
Cdd:cd14075  241 SDRYSIDEIKNSEWL 255
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
53-303 6.04e-108

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: 331.66  E-value: 6.04e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS-LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQdMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCeNLLKKFLILNPSK 291
Cdd:cd14073  163 SPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSDAS-GLIRWMLTVNPKR 241
                        250
                 ....*....|..
gi 564332436 292 RGTLEQIMKDRW 303
Cdd:cd14073  242 RATIEDIANHWW 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
51-304 4.53e-107

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: 329.37  E-value: 4.53e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14074    3 GLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN-IKIADFGFSNEFTFGNKLDT 208
Cdd:cd14074   83 LGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQPGEKLET 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14074  163 SCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRD 242
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14074  243 PKKRASLEEIENHPWL 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-303 1.71e-104

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: 322.82  E-value: 1.71e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEqIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS---NEFTFGNKLDT 208
Cdd:cd14663   82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalsEQFRQDGLLHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14663  162 TCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPN 241
                        250
                 ....*....|....*
gi 564332436 289 PSKRGTLEQIMKDRW 303
Cdd:cd14663  242 PSTRITVEQIMASPW 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
51-304 4.11e-103

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: 319.33  E-value: 4.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14078    3 KYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAL-GDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK--LDT 208
Cdd:cd14078   82 YCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDhhLET 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14078  162 CCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVD 241
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14078  242 PKKRITVKELLNHPWV 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
51-304 3.18e-99

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: 309.38  E-value: 3.18e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKT-------------QLNSSSLQKLFREVRIMKVLNHPNIVKLFE 117
Cdd:cd14077    1 GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRAsnaglkkerekrlEKEISRDIRTIREAALSSLLNHPHICRLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 118 VIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS 197
Cdd:cd14077   81 FLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 NEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDC 277
Cdd:cd14077  161 NLYDPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSEC 240
                        250       260
                 ....*....|....*....|....*..
gi 564332436 278 ENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14077  241 KSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
53-304 3.84e-98

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: 306.42  E-value: 3.84e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLA--RHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKFLpRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL--- 206
Cdd:cd14080   82 EYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDvls 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP---FYMSTDCENLLKK 283
Cdd:cd14080  162 KTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECKDLIDQ 241
                        250       260
                 ....*....|....*....|.
gi 564332436 284 FLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14080  242 LLEPDPTKRATIEEILNHPWL 262
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
55-304 3.88e-93

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: 292.84  E-value: 3.88e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd14007    4 IGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLrREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFgNKLDTFCGSP 213
Cdd:cd14007   84 NGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPS-NRRKTFCGTL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRG 293
Cdd:cd14007  163 DYLPPEMVEGKEYD-YKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKRL 241
                        250
                 ....*....|.
gi 564332436 294 TLEQIMKDRWM 304
Cdd:cd14007  242 SLEQVLNHPWI 252
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
53-304 3.38e-89

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: 282.61  E-value: 3.38e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHiLTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRIkDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQTYCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCeNLLKKFLILNPSK 291
Cdd:cd14161  164 SPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSDAC-GLIRWLLMVNPER 242
                        250
                 ....*....|...
gi 564332436 292 RGTLEQIMKDRWM 304
Cdd:cd14161  243 RATLEDVASHWWV 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
53-303 4.66e-86

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: 274.56  E-value: 4.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKfLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGF-----SNEFTFGNKL 206
Cdd:cd14162   82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFargvmKTKDGKPKLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRgkyRIPF----YMSTDCENLLK 282
Cdd:cd14162  162 ETYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR---RVVFpknpTVSEECKDLIL 238
                        250       260
                 ....*....|....*....|.
gi 564332436 283 KFLILNPsKRGTLEQIMKDRW 303
Cdd:cd14162  239 RMLSPVK-KRITIEEIKRDPW 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
59-304 1.84e-84

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: 270.58  E-value: 1.84e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLN------------SSSLQKLFREVRIMKVLNHPNIVKLFEVIE--TEKT 124
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRkrregkndrgkiKNALDDVRREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDYLVAHGR--MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:cd14008   81 LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GN-KLDTFCGSPPYAAPELFQG--KKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF--YMSTDC 277
Cdd:cd14008  161 GNdTLQKTAGTPAFLAPELCDGdsKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIppELSPEL 240
                        250       260
                 ....*....|....*....|....*..
gi 564332436 278 ENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14008  241 KDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
59-304 3.25e-83

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: 266.69  E-value: 3.25e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEhTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDTFCGSPPYA 216
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGdRTYTFCGTPEYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 217 APELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR---G 293
Cdd:cd05123  161 APEVLLGKGY-GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRlgsG 239
                        250
                 ....*....|.
gi 564332436 294 TLEQIMKDRWM 304
Cdd:cd05123  240 GAEEIKAHPFF 250
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
59-296 5.61e-80

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: 257.92  E-value: 5.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNEFTFGNKLDTFCGSPPY 215
Cdd:cd14009   81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASMAETLCGSPLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKFLILNPSK 291
Cdd:cd14009  161 MAPEILQFQKYDA-KADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFpiaaQLSPDCKDLLRRLLRRDPAE 239

                 ....*
gi 564332436 292 RGTLE 296
Cdd:cd14009  240 RISFE 244
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
52-300 3.32e-79

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: 256.24  E-value: 3.32e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL----VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS----NEFTFG 203
Cdd:cd08215   81 ADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISkvleSTTDLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NkldTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCENLLK 282
Cdd:cd08215  161 K---TVVGTPYYLSPELCENKPYNYK-SDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVN 236
                        250
                 ....*....|....*...
gi 564332436 283 KFLILNPSKRGTLEQIMK 300
Cdd:cd08215  237 SMLQKDPEKRPSANEILS 254
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
51-304 7.51e-79

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: 255.87  E-value: 7.51e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHI-----LTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKT 124
Cdd:cd14076    1 GPYILGRTLGEGEFGKVKLGWPLpkanhRSGVQVAIKLIRRdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF--TF 202
Cdd:cd14076   81 IGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdhFN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKK-YDGPEVDVWSLGVILYTLVSGSLPFD-------GQNLKELRERVLRGKYRIPFYMS 274
Cdd:cd14076  161 GDLMSTSCGSPCYAAPELVVSDSmYAGRKADIWSCGVILYAMLAGYLPFDddphnpnGDNVPRLYRYICNTPLIFPEYVT 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 275 TDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14076  241 PKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
53-304 4.35e-77

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: 250.55  E-value: 4.35e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF-GNKLDTFC 210
Cdd:cd14099   83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYdGERKKTLC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY--MSTDCENLLKKFLILN 288
Cdd:cd14099  163 GTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlsISDEAKDLIRSMLQPD 242
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14099  243 PTKRPSLDEILSHPFF 258
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
50-304 1.54e-75

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: 246.65  E-value: 1.54e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS--LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYL 127
Cdd:cd14070    1 VGSYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF---GN 204
Cdd:cd14070   81 VMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGIlgySD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF--DGQNLKELRERVLRGKYR-IPFYMSTDCENLL 281
Cdd:cd14070  161 PFSTQCGSPAYAAPELLARKKY-GPKVDVWSIGVNMYAMLTGTLPFtvEPFSLRALHQKMVDKEMNpLPTDLSPGAISFL 239
                        250       260
                 ....*....|....*....|...
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14070  240 RSLLEPDPLKRPNIKQALANRWL 262
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
53-303 1.61e-74

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: 243.78  E-value: 1.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK---LDTF 209
Cdd:cd14069   83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKerlLNKM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG--------QNLKELRERVLRGKYRIpfymSTDCENLL 281
Cdd:cd14069  163 CGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQpsdscqeySDWKENKKTYLTPWKKI----DTAALSLL 238
                        250       260
                 ....*....|....*....|..
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14069  239 RKILTENPNKRITIEDIKKHPW 260
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
59-301 6.18e-74

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: 240.64  E-value: 6.18e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKtQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPK-EKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG--SPPY 215
Cdd:cd00180   80 DLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGgtTPPY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKKYDGPEVDVWSLGVILYTLvsgslpfdgqnlkelrervlrgkyripfymsTDCENLLKKFLILNPSKRGTL 295
Cdd:cd00180  160 YAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRPSA 208

                 ....*.
gi 564332436 296 EQIMKD 301
Cdd:cd00180  209 KELLEH 214
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
53-304 1.96e-71

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: 235.45  E-value: 1.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFEVIET-EKTLYLVME 130
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKfLPRELEILARLNHKSIIKTYEIFETsDGKVYIVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK----- 205
Cdd:cd14165   83 LGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENgrivl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP--FYMSTDCENLLKK 283
Cdd:cd14165  163 SKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPrsKNLTSECKDLIYR 242
                        250       260
                 ....*....|....*....|.
gi 564332436 284 FLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14165  243 LLQPDVSQRLCIDEVLSHPWL 263
Pkinase pfam00069
Protein kinase domain;
53-304 4.59e-70

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 230.21  E-value: 4.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVqychqkfivhrdlkaENllldadmnikiadfgfsneftfGNKLDTFCGS 212
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL---------------ES----------------------GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  213 PPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PFYMSTDCENLLKKFLILNP 289
Cdd:pfam00069 124 PWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFpelPSNLSEEAKDLLKKLLKKDP 202
                         250
                  ....*....|....*
gi 564332436  290 SKRGTLEQIMKDRWM 304
Cdd:pfam00069 203 SKRLTATQALQHPWF 217
MARK2_C cd12201
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
742-840 1.16e-69

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 2; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK2, also called Par-1b or ELKL motif kinase 1 (EMK-1), is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. It also regulates axon formation and has been implicated in neurodegeneration. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213386  Cd Length: 99  Bit Score: 224.54  E-value: 1.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 742 KPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRI 821
Cdd:cd12201    1 KPRSLRFTWSMKTTSSMEPNEMMKEIRKVLDANNCQYELQEKYMLLCMHGTPGHDDFVQWEMEVCKLPRLSLNGVRFKRI 80
                         90
                 ....*....|....*....
gi 564332436 822 SGTSMAFKNIASKIANELK 840
Cdd:cd12201   81 SGTSIAFKNIASKIANELK 99
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
52-270 4.54e-69

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: 229.01  E-value: 4.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFlREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG--NKLDT 208
Cdd:cd14014   81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSglTQTGS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332436 209 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP 270
Cdd:cd14014  161 VLGTPAYMAPEQARGGPVD-PRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPP 221
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
53-304 2.39e-68

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: 227.66  E-value: 2.39e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQ------KLFREVRIMKVLNHPNIVKLFEVIETEKTLY 126
Cdd:cd14084    8 YIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRReinkprNIETEIEILKKLSHPCIIKIEDFFDAEDDYY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFG 203
Cdd:cd14084   88 IVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSKILGET 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NKLDTFCGSPPYAAPELFQ--GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLK-ELRERVLRGKYR-IPFY---MSTD 276
Cdd:cd14084  168 SLMKTLCGTPTYLAPEVLRsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQmSLKEQILSGKYTfIPKAwknVSEE 247
                        250       260
                 ....*....|....*....|....*...
gi 564332436 277 CENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14084  248 AKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
52-292 4.14e-66

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: 221.70  E-value: 4.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05581    2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYvTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG--------------- 195
Cdd:cd05581   82 YAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvlgpdsspestk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 ---FSNEFTFGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY 272
Cdd:cd05581  162 gdaDSQIAYNQARAASFVGTAEYVSPELLNEKPA-GKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPEN 240
                        250       260
                 ....*....|....*....|
gi 564332436 273 MSTDCENLLKKFLILNPSKR 292
Cdd:cd05581  241 FPPDAKDLIQKLLVLDPSKR 260
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
53-304 4.19e-66

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: 221.11  E-value: 4.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS------LQKLFREVRIMKVLN---HPNIVKLFEVIETEK 123
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTwvrdrkLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVME-YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGfSNEFTF 202
Cdd:cd14004   82 FYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG-SAAYIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFdgQNLKElrerVLRGKYRIPFYMSTDCENLLK 282
Cdd:cd14004  161 SGPFDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPF--YNIEE----ILEADLRIPYAVSEDLIDLIS 234
                        250       260
                 ....*....|....*....|..
gi 564332436 283 KFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14004  235 RMLNRDVGDRPTIEELLTDPWL 256
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-303 1.33e-65

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: 219.55  E-value: 1.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS--SSLQKlfrEVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGkeDSLEN---EIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL---LDADMNIKIADFGFSnEFTFGNKLD 207
Cdd:cd14083   82 LVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLS-KMEDSGVMS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKK 283
Cdd:cd14083  161 TACGTPGYVAPEVLAQKPY-GKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFdsPYWddISDSAKDFIRH 239
                        250       260
                 ....*....|....*....|
gi 564332436 284 FLILNPSKRGTLEQIMKDRW 303
Cdd:cd14083  240 LMEKDPNKRYTCEQALEHPW 259
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
52-303 2.90e-65

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: 219.76  E-value: 2.90e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05580    2 DFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKLDTFC 210
Cdd:cd05580   82 YVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK--DRTYTLC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:cd05580  160 GTPEYLAPEIILSKGHGKA-VDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLT 238
                        250
                 ....*....|....*...
gi 564332436 291 KR-GTL----EQIMKDRW 303
Cdd:cd05580  239 KRlGNLkngvEDIKNHPW 256
MARK1-3_C cd12196
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
742-839 3.65e-65

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases 1-3; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK1/2, through their activation by death-associated protein kinase (DAPK), modulates polarized neurite outgrowth. MARK1, also called Par-1c, is also involved in axon-dendrite specification, and SNPs on the MARK1 gene is associated with autism spectrum disorders. MARK2, also called Par-1b, is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. MARK3, also called Par-1a, is implicated in gluconeogenesis and adiposity; mice deficient with MARK3 display reduced adiposity, resistance to hepatic steatosis, and defective gluconeogensis. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213381  Cd Length: 98  Bit Score: 212.31  E-value: 3.65e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 742 KPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRI 821
Cdd:cd12196    1 KPRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQRERFLLFCVHGDGRTDSLVQWEMEVCKLPRLSLNGVRFKRI 80
                         90
                 ....*....|....*...
gi 564332436 822 SGTSMAFKNIASKIANEL 839
Cdd:cd12196   81 SGTSIAFKNIASKIANEL 98
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
52-304 5.18e-65

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: 218.76  E-value: 5.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS------LQKLFREVRIMKVLN-HPNIVKLFEVIETEKT 124
Cdd:cd14093    4 KYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSEneaeelREATRREIEILRQVSgHPNIIELHDVFESPTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN 204
Cdd:cd14093   84 IFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYD-----GPEVDVWSLGVILYTLVSGSLPF-DGQNLKELReRVLRGKYRI--PFY--MS 274
Cdd:cd14093  164 KLRELCGTPGYLAPEVLKCSMYDnapgyGKEVDMWACGVIMYTLLAGCPPFwHRKQMVMLR-NIMEGKYEFgsPEWddIS 242
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 275 TDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14093  243 DTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
53-303 1.24e-64

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: 217.34  E-value: 1.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ--LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL--DADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14098   82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAKVIHTGTFLVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPE-----VDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP----FYMSTDCEN 279
Cdd:cd14098  162 FCGTMAYLAPEILMSKEQNLQGgysnlVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPplvdFNISEEAID 241
                        250       260
                 ....*....|....*....|....
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14098  242 FILRLLDVDPEKRMTAAQALDHPW 265
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-303 1.64e-64

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: 216.56  E-value: 1.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQklfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQ---REIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM--NIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd14662   79 AGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKSTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPF----DGQNLKELRERVLRGKYRIPFY--MSTDCENLLKKF 284
Cdd:cd14662  159 GTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFedpdDPKNFRKTIQRIMSVQYKIPDYvrVSQDCRHLLSRI 238
                        250
                 ....*....|....*....
gi 564332436 285 LILNPSKRGTLEQIMKDRW 303
Cdd:cd14662  239 FVANPAKRITIPEIKNHPW 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
50-292 2.48e-64

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 223.74  E-value: 2.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFrREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN--KL 206
Cdd:COG0515   86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATltQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDC----ENLLK 282
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVD-PRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLppalDAIVL 244
                        250
                 ....*....|
gi 564332436 283 KFLILNPSKR 292
Cdd:COG0515  245 RALAKDPEER 254
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
53-304 1.42e-63

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: 214.08  E-value: 1.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIE-TEKTLYLVME 130
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLEsADGKIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAdMNIKIADFGFSNEFTFGNK--LDT 208
Cdd:cd14163   82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQG-FTLKLTDFGFAKQLPKGGRelSQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGkYRIPFYM--STDCENLLKKFLI 286
Cdd:cd14163  161 FCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG-VSLPGHLgvSRTCQDLLKRLLE 239
                        250
                 ....*....|....*...
gi 564332436 287 LNPSKRGTLEQIMKDRWM 304
Cdd:cd14163  240 PDMVLRPSIEEVSWHPWL 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
59-300 1.99e-63

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: 213.17  E-value: 1.99e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHIltGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLvaHGRMKE--KEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-NEFTFGNKLDTFCGSPP 214
Cdd:cd13999   79 DLL--HKKKIPlsWSLRLKIaLDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSrIKNSTTEKMTGVVGTPR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR--IPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd13999  157 WMAPEVLRGEPYT-EKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRppIPPDCPPELSKLIKRCWNEDPEKR 235

                 ....*...
gi 564332436 293 GTLEQIMK 300
Cdd:cd13999  236 PSFSEIVK 243
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-303 2.30e-63

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: 213.69  E-value: 2.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQklfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQ---REIINHRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM--NIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd14665   79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKSTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPF----DGQNLKELRERVLRGKYRIPFY--MSTDCENLLKKF 284
Cdd:cd14665  159 GTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFedpeEPRNFRKTIQRILSVQYSIPDYvhISPECRHLISRI 238
                        250
                 ....*....|....*....
gi 564332436 285 LILNPSKRGTLEQIMKDRW 303
Cdd:cd14665  239 FVADPATRITIPEIRNHEW 257
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
52-304 2.62e-63

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: 214.59  E-value: 2.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14086    2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFT------F 202
Cdd:cd14086   82 VTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQgdqqawF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GnkldtFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCE 278
Cdd:cd14086  162 G-----FAGTPGYLSPEVLRKDPYGKP-VDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAK 235
                        250       260
                 ....*....|....*....|....*.
gi 564332436 279 NLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14086  236 DLINQMLTVNPAKRITAAEALKHPWI 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
53-303 2.97e-63

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: 213.34  E-value: 2.97e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSslQKLFR-EVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGK--EHMIEnEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL----DADMNIKIADFGFSNEFTfgNKLD 207
Cdd:cd14095   80 VKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATEVK--EPLF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF--DGQNLKELRERVLRGKYRI--PFY--MSTDCENLL 281
Cdd:cd14095  158 TVCGTPTYVAPEILAETGY-GLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEFEFlsPYWdnISDSAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14095  237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
59-304 1.25e-62

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: 211.35  E-value: 1.25e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS--SSLQKLFREVRIMKVLNHPNIVKLFEVI---ETEKtLYLVMEYAS 133
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRipNGEANVKREIQILRRLNHRNVIKLVDVLyneEKQK-LYMVMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GG--EVFDYLVAHgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE---FTFGNKLDT 208
Cdd:cd14119   80 GGlqEMLDSAPDK-RLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAldlFAEDDTCTT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKK-YDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLIL 287
Cdd:cd14119  159 SQGSPAFQPPEIANGQDsFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEK 238
                        250
                 ....*....|....*..
gi 564332436 288 NPSKRGTLEQIMKDRWM 304
Cdd:cd14119  239 DPEKRFTIEQIRQHPWF 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
52-292 2.83e-62

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: 210.57  E-value: 2.83e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK-LDTFC 210
Cdd:cd14002   82 AQ-GELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLvLTSIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:cd14002  161 GTPLYMAPELVQEQPYD-HTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDPS 239

                 ..
gi 564332436 291 KR 292
Cdd:cd14002  240 KR 241
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
52-302 3.65e-62

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: 210.48  E-value: 3.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLF--EVIETEKTLYLVM 129
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYdrIVDRANTTLYIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAK----FRQIVSAVQYCH-----QKFIVHRDLKAENLLLDADMNIKIADFGFSNEF 200
Cdd:cd08217   81 EYCEGGDLAQLIKKCKKENQYIPEEFiwkiFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLARVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TFGNKL-DTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCE 278
Cdd:cd08217  161 SHDSSFaKTYVGTPYYMSPELLNEQSYD-EKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFpRIPSRYSSELN 239
                        250       260
                 ....*....|....*....|....
gi 564332436 279 NLLKKFLILNPSKRGTLEQIMKDR 302
Cdd:cd08217  240 EVIKSMLNVDPDKRPSVEELLQLP 263
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
53-303 5.28e-62

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: 209.75  E-value: 5.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd05122   80 SGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTFVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFdgQNLKELR--ERVLRG---KYRIPFYMSTDCENLLKKFLI 286
Cdd:cd05122  160 TPYWMAPEVIQGKPYG-FKADIWSLGITAIEMAEGKPPY--SELPPMKalFLIATNgppGLRNPKKWSKEFKDFLKKCLQ 236
                        250
                 ....*....|....*..
gi 564332436 287 LNPSKRGTLEQIMKDRW 303
Cdd:cd05122  237 KDPEKRPTAEQLLKHPF 253
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
59-305 1.28e-61

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: 209.00  E-value: 1.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAA 217
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWTFCGTPEYVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 218 PELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELR--ERVLRGKYRI--PFYMSTDCENLLKKFLILNPSKR- 292
Cdd:cd05572  161 PEIILNKGYD-FSVDYWSLGILLYELLTGRPPFGGDDEDPMKiyNIILKGIDKIefPKYIDKNAKNLIKQLLRRNPEERl 239
                        250
                 ....*....|....*..
gi 564332436 293 ----GTLEQIMKDRWMN 305
Cdd:cd05572  240 gylkGGIRDIKKHKWFE 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
53-303 1.92e-61

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: 208.26  E-value: 1.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL----DADMNIKIADFGFSNEFTfgNKLDT 208
Cdd:cd14185   81 RGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT--GPIFT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQ--NLKELRERVLRGKYRI--PFY--MSTDCENLLK 282
Cdd:cd14185  159 VCGTPTYVAPEILSEKGY-GLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEFlpPYWdnISEAAKDLIS 237
                        250       260
                 ....*....|....*....|.
gi 564332436 283 KFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14185  238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
59-303 2.70e-61

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: 208.61  E-value: 2.70e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMiRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS--------NEFTFGNKLD-- 207
Cdd:cd05579   81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrrqIKLSIQKKSNga 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 ------TFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP--FYMSTDCEN 279
Cdd:cd05579  161 pekedrRIVGTPDYLAPEILLGQGH-GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPedPEVSDEAKD 239
                        250       260
                 ....*....|....*....|....*..
gi 564332436 280 LLKKFLILNPSKR---GTLEQIMKDRW 303
Cdd:cd05579  240 LISKLLTPDPEKRlgaKGIEEIKNHPF 266
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
53-304 1.13e-60

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: 206.25  E-value: 1.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFEVIE-TEKTLYLVME 130
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKfLPRELSILRRVNHPNIVQMFECIEvANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 yASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFGFSNEFTFGNKLD-T 208
Cdd:cd14164   82 -AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADdRKIKIADFGFARFVEDYPELStT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14164  161 FCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVALEEPCRALIRTLLQFN 240
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14164  241 PSTRPSIQQVAGNSWL 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
52-303 4.47e-60

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: 204.68  E-value: 4.47e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS---NEFTFGNKLDT 208
Cdd:cd06606   81 VPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAkrlAEIATGEGTKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRGKY--RIPFYMSTDCENLLKKFL 285
Cdd:cd06606  161 LRGTPYWMAPEVIRGEGY-GRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGEppPIPEHLSEEAKDFLRKCL 239
                        250
                 ....*....|....*...
gi 564332436 286 ILNPSKRGTLEQIMKDRW 303
Cdd:cd06606  240 QRDPKKRPTADELLQHPF 257
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
59-303 1.29e-59

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: 202.88  E-value: 1.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQklfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVL---REISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLD--ADMNIKIADFGFSNEFTFGNKLDTFCGSPPYA 216
Cdd:cd14006   78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGEELKEIFGTPEFV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 217 APELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYM----STDCENLLKKFLILNPSKR 292
Cdd:cd14006  158 APEIVNGEPV-SLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYfssvSQEAKDFIRKLLVKEPRKR 236
                        250
                 ....*....|.
gi 564332436 293 GTLEQIMKDRW 303
Cdd:cd14006  237 PTAQEALQHPW 247
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
52-304 4.97e-59

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: 203.05  E-value: 4.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHI-LTGKEVAVKIIDKTQLNSSSLQ-----KLFREVRIMKVLNHPNIVKLFEVIETEKTL 125
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVRKADLSSDNLKgssraNILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL---------------LDADMN-- 188
Cdd:cd14096   82 YIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkADDDETkv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 189 ----------------IKIADFGFSNEFtFGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd14096  162 degefipgvggggigiVKLADFGLSKQV-WDSNTKTPCGTVGYTAPEVVKDERYS-KKVDMWALGCVLYTLLCGFPPFYD 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 253 QNLKELRERVLRGKYRI--PFY--MSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14096  240 ESIETLTEKISRGDYTFlsPWWdeISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
53-304 2.31e-58

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: 200.94  E-value: 2.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlqklfrEVRI-MKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSE------EIEIlLRYGQHPNIITLRDVYDDGNSVYLVTEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLdADM-----NIKIADFGFSNEFTFGNK- 205
Cdd:cd14091   76 LRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILY-ADEsgdpeSLRICDFGFAKQLRAENGl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPF-----DGQNlkELRERVlrGKYRIPF------YMS 274
Cdd:cd14091  155 LMTPCYTANFVAPEVLKKQGYDA-ACDIWSLGVLLYTMLAGYTPFasgpnDTPE--VILARI--GSGKIDLsggnwdHVS 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 275 TDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14091  230 DSAKDLVRKMLHVDPSQRPTAAQVLQHPWI 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
59-297 3.98e-58

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: 199.05  E-value: 3.98e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKE-VAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14121    3 LGSGTYATVYKAYRKSGAREvVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN--IKIADFGFSNEFTFGNKLDTFCGSPPY 215
Cdd:cd14121   83 SRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNpvLKLADFGFAQHLKPNDEAHSLRGSPLY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGK-YRIPFY--MSTDCENLLKKFLILNPSKR 292
Cdd:cd14121  163 MAPEMILKKKYD-ARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQRDPDRR 241

                 ....*
gi 564332436 293 GTLEQ 297
Cdd:cd14121  242 ISFEE 246
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
59-304 4.53e-58

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: 199.46  E-value: 4.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEV--AVKIIDKTQLNSSSLQ---KLFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVMEYA 132
Cdd:cd13994    1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRRRDDESKRKDyvkRLTSEYIISSKLHHPNIVKVLDLCQDLHgKWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-TFGNKL----D 207
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFgMPAEKEspmsA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPF-----DGQNLK--ELRERVLRGKYRIPFY-MSTDCEN 279
Cdd:cd13994  161 GLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWrsakkSDSAYKayEKSGDFTNGPYEPIENlLPSECRR 240
                        250       260
                 ....*....|....*....|....*
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd13994  241 LIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
52-319 8.45e-58

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: 199.58  E-value: 8.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS-SSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRlKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKLDTFC 210
Cdd:cd05612   82 YVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR--DRTWTLC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:cd05612  160 GTPEYLAPEVIQSKGH-NKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRT 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 291 KR-GTL----EQIMKDRWMNVGHEDD----ELKPYVEP 319
Cdd:cd05612  239 RRlGNMkngaDDVKNHRWFKSVDWDDvpqrKLKPPIVP 276
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
57-292 1.71e-57

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: 199.75  E-value: 1.71e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEViIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKeaRAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDTFCG 211
Cdd:cd05570   81 GDLMFHIQRARRFTEE--RARFyaAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEgIWGGNTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSK 291
Cdd:cd05570  159 TPDYIAPEILREQDY-GFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPAR 237

                 .
gi 564332436 292 R 292
Cdd:cd05570  238 R 238
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
52-304 6.51e-57

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: 195.92  E-value: 6.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ----LNSSSLQKLFREVRIMKVLN---HPNIVKLFEVIETEKT 124
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewAMINGPVPVPLEIALLLKASkpgVPGVIRLLDWYERPDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGE-VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFGFSNEFTF 202
Cdd:cd14005   81 FLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFGCGALLKD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKlDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFdgqnlkELRERVLRGKYRIPFYMSTDCENLLK 282
Cdd:cd14005  161 SVY-TDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPF------ENDEQILRGNVLFRPRLSKECCDLIS 233
                        250       260
                 ....*....|....*....|..
gi 564332436 283 KFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14005  234 RCLQFDPSKRPSLEQILSHPWF 255
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
52-307 7.26e-57

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: 197.52  E-value: 7.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRL---LKTIGKGNFAKVKLARHILTGKEVAVKIIDKtQLNSSslqklfREVRIMKVL-NHPNIVKLFEVIETEKTLYL 127
Cdd:cd14092    4 NYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSR-RLDTS------REVQLLRLCqGHPNIVKLHEVFQDELHTYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGN 204
Cdd:cd14092   77 VMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPE-LFQGKKYDG--PEVDVWSLGVILYTLVSGSLPFDGQNLK----ELRERVLRGKYRIPFY----M 273
Cdd:cd14092  157 PLKTPCFTLPYAAPEvLKQALSTQGydESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFDGEewknV 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564332436 274 STDCENLLKKFLILNPSKRGTLEQIMKDRWMNVG 307
Cdd:cd14092  237 SSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGS 270
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
59-303 7.33e-56

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: 193.73  E-value: 7.33e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQL---------------------NSSSLQKLFREVRIMKVLNHPNIVKLFE 117
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrkpgalgkPLDPLDRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 118 VIE--TEKTLYLVMEYASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG 195
Cdd:cd14118   82 VLDdpNEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 FSNEFTFGN-KLDTFCGSPPYAAPELFQG--KKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP-- 270
Cdd:cd14118  161 VSNEFEGDDaLLSSTAGTPAFMAPEALSEsrKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPdd 240
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 271 FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14118  241 PVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-304 8.14e-56

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: 193.57  E-value: 8.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA---DMNIKIADFGFSnEFTFGNKLDTF 209
Cdd:cd14169   84 TGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLS-KIEAQGMLSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKKFL 285
Cdd:cd14169  163 CGTPGYVAPELLEQKPY-GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFdsPYWddISESAKDFIRHLL 241
                        250
                 ....*....|....*....
gi 564332436 286 ILNPSKRGTLEQIMKDRWM 304
Cdd:cd14169  242 ERDPEKRFTCEQALQHPWI 260
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-311 2.83e-55

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: 192.51  E-value: 2.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlqKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDS--SLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGnKLDTF 209
Cdd:cd14166   83 SGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQNG-IMSTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKKFL 285
Cdd:cd14166  162 CGTPGYVAPEVLAQKPYS-KAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFesPFWddISESAKDFIRHLL 240
                        250       260
                 ....*....|....*....|....*...
gi 564332436 286 ILNPSKRGTLEQIMKDRWM--NVGHEDD 311
Cdd:cd14166  241 EKNPSKRYTCEKALSHPWIigNTALHRD 268
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
53-304 3.24e-55

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: 191.21  E-value: 3.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlfrEVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCES---ELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFG--NKLD 207
Cdd:cd14087   80 TGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGpnCLMK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKF--- 284
Cdd:cd14087  160 TTCGTPEYIAPEILLRKPYTQ-SVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFidr 238
                        250       260
                 ....*....|....*....|.
gi 564332436 285 -LILNPSKRGTLEQIMKDRWM 304
Cdd:cd14087  239 lLTVNPGERLSATQALKHPWI 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
52-292 1.43e-54

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: 190.69  E-value: 1.43e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVvKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKLDTFC 210
Cdd:cd14209   82 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVK--GRTWTLC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:cd14209  160 GTPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLT 238

                 ..
gi 564332436 291 KR 292
Cdd:cd14209  239 KR 240
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
52-304 3.61e-54

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: 188.70  E-value: 3.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14167    4 IYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE-TSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL---LDADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14167   83 VSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEGSGSVMST 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKKF 284
Cdd:cd14167  163 ACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFdsPYWddISDSAKDFIQHL 241
                        250       260
                 ....*....|....*....|
gi 564332436 285 LILNPSKRGTLEQIMKDRWM 304
Cdd:cd14167  242 MEKDPEKRFTCEQALQHPWI 261
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
59-292 4.14e-54

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: 187.96  E-value: 4.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHI-LTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14120    1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNL-SKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLD---------ADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14120   80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShnsgrkpspNDIRLKIADFGFARFLQDGMMAAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELR---ERVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd14120  160 LCGSPMYMAPEVIMSLQYDA-KADLWSIGTIVYQCLTGKAPFQAQTPQELKafyEKNANLRPNIPSGTSPALKDLLLGLL 238

                 ....*..
gi 564332436 286 ILNPSKR 292
Cdd:cd14120  239 KRNPKDR 245
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
57-292 5.65e-54

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: 189.87  E-value: 5.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEViIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDTFCGSPP 214
Cdd:cd05571   81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEeISYGATTKTFCGTPE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 215 YAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05571  161 YLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
52-301 2.20e-53

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 188.49  E-value: 2.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKLDTFC 210
Cdd:PTZ00263  99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP--DRTFTLC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:PTZ00263 177 GTPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHT 255
                        250
                 ....*....|..
gi 564332436 291 KR-GTLEQIMKD 301
Cdd:PTZ00263 256 KRlGTLKGGVAD 267
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
53-305 2.42e-53

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: 185.88  E-value: 2.42e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDktqLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMR---LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFC 210
Cdd:cd06614   79 DGGSLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEkSKRNSVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENL 280
Cdd:cd06614  159 GTPYWMAPEVIKRKDYG-PKVDIWSLGIMCIEMAEGEPPY-------LEEPPLRALFLIttkgipplknPEKWSPEFKDF 230
                        250       260
                 ....*....|....*....|....*
gi 564332436 281 LKKFLILNPSKRGTLEQIMKDRWMN 305
Cdd:cd06614  231 LNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
52-299 4.12e-53

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: 185.89  E-value: 4.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-------FREVRIM-KVLNHPNIVKLFEVIETEK 123
Cdd:cd14182    4 KYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEVqelreatLKEIDILrKVSGHPNIIQLKDTYETNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG 203
Cdd:cd14182   84 FFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NKLDTFCGSPPYAAPELFQGKKYD-----GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MS 274
Cdd:cd14182  164 EKLREVCGTPGYLAPEIIECSMDDnhpgyGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPEWddRS 243
                        250       260
                 ....*....|....*....|....*
gi 564332436 275 TDCENLLKKFLILNPSKRGTLEQIM 299
Cdd:cd14182  244 DTVKDLISRFLVVQPQKRYTAEEAL 268
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
52-304 4.17e-53

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: 185.55  E-value: 4.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQ-KLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14116    6 DFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEhQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEfTFGNKLDTFC 210
Cdd:cd14116   86 YAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH-APSSRRTTLC 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:cd14116  165 GTLDYLPPEMIEGRMHD-EKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPS 243
                        250
                 ....*....|....
gi 564332436 291 KRGTLEQIMKDRWM 304
Cdd:cd14116  244 QRPMLREVLEHPWI 257
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-304 6.15e-53

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: 186.18  E-value: 6.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlnssSLQKLFR-EVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT-----VDKKIVRtEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL---LDADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14085   80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKIVDQQVTMKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKK 283
Cdd:cd14085  160 VCGTPGYCAPEILRGCAY-GPEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDYDFvsPWWddVSLNAKDLVKK 238
                        250       260
                 ....*....|....*....|.
gi 564332436 284 FLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14085  239 LIVLDPKKRLTTQQALQHPWV 259
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
53-304 6.85e-53

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: 185.38  E-value: 6.85e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS----SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAEN-LLLDADM---NIKIADFGFSNEFTFGN 204
Cdd:cd14105   87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNVpipRIKLIDFGLAHKIEDGN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY----RIPFYMSTDCE 278
Cdd:cd14105  167 EFKNIFGTPEFVAPEIVN---YEplGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYdfddEYFSNTSELAK 243
                        250       260
                 ....*....|....*....|....*.
gi 564332436 279 NLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14105  244 DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
52-299 8.51e-53

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: 184.55  E-value: 8.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGR--MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNI-KIADFGFSNEFTFGNKLDT 208
Cdd:cd08220   81 APGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKSKAYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCENLLKKFLIL 287
Cdd:cd08220  161 VVGTPCYISPELCEGKPYN-QKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHL 239
                        250
                 ....*....|..
gi 564332436 288 NPSKRGTLEQIM 299
Cdd:cd08220  240 DPNKRPTLSEIM 251
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
53-303 2.09e-52

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: 184.22  E-value: 2.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLN----SSSLqklfREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipSTAL----REISLLKELKHPNIVKLLDVIHTENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASggevFD---YL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN 204
Cdd:cd07829   77 FEYCD----QDlkkYLdKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTfcgsPP-----YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQ----------------------NLKE 257
Cdd:cd07829  153 RTYT----HEvvtlwYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDseidqlfkifqilgtpteeswpGVTK 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 258 LRErvlrGKYRIPFYMSTDCE-----------NLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07829  229 LPD----YKPTFPKWPKNDLEkvlprldpegiDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
52-304 3.20e-52

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: 182.75  E-value: 3.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSL-QKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDT 208
Cdd:cd14186   82 MCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHeKHFT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELfQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14186  162 MCGTPNYISPEI-ATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14186  241 PADRLSLSSVLDHPFM 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
52-300 7.90e-52

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: 184.80  E-value: 7.90e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR-IMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERdILADADSPWIVRLHYAFQDEDHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS------------- 197
Cdd:cd05573   82 YMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkmnksgdresyl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 ----------NEFTFGNKLD-------TFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRE 260
Cdd:cd05573  162 ndsvntlfqdNVLARRRPHKqrrvraySAVGTPDYIAPEVLRGTGY-GPECDWWSLGVILYEMLYGFPPFYSDSLVETYS 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564332436 261 RVLRGK--YRIPFY--MSTDCENLLKKFLIlNPSKR-GTLEQIMK 300
Cdd:cd05573  241 KIMNWKesLVFPDDpdVSPEAIDLIRRLLC-DPEDRlGSAEEIKA 284
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
52-304 9.44e-52

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: 181.69  E-value: 9.44e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05578    1 HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKcIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEkeARAKFR--QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd05578   81 LLLGGDLRYHLQQKVKFSE--ETVKFYicEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLK---ELRERVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd05578  159 TSGTKPYMAPEVFMRAGY-SFAVDWWSLGVTAYEMLRGKRPYEIHSRTsieEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                        250       260
                 ....*....|....*....|
gi 564332436 286 ILNPSKR-GTLEQIMKDRWM 304
Cdd:cd05578  238 ERDPQKRlGDLSDLKNHPYF 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
52-299 5.19e-51

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: 179.51  E-value: 5.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMK----EKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLD 207
Cdd:cd08530   81 APFGDLSKLISKRKKKRrlfpEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK-KNLAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCENLLKKFLI 286
Cdd:cd08530  160 TQIGTPLYAAPEVWKGRPYDYKS-DIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFpPIPPVYSQDLQQIIRSLLQ 238
                        250
                 ....*....|...
gi 564332436 287 LNPSKRGTLEQIM 299
Cdd:cd08530  239 VNPKKRPSCDKLL 251
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
57-304 9.61e-51

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: 179.08  E-value: 9.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKV-LNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd14106   14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELcKDCPRVVNLHEVYETRSELILILELAAGG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:cd14106   94 ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVIGEGEEIREILGT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP---FY-MSTDCENLLKKFLI 286
Cdd:cd14106  174 PDYVAPEILS---YEpiSLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPeelFKdVSPLAIDFIKRLLV 250
                        250
                 ....*....|....*...
gi 564332436 287 LNPSKRGTLEQIMKDRWM 304
Cdd:cd14106  251 KDPEKRLTAKECLEHPWL 268
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
57-402 1.02e-50

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: 180.97  E-value: 1.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKeVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDTFCGSPP 214
Cdd:cd05595   81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgITDGATMKTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR-- 292
Cdd:cd05595  161 YLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRlg 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 293 ---GTLEQIMKDRWMNVGHEDDELKPYVepLPDYKdPRRTelmvsmgytreeiqdSLVGQRYNEvmatylllgyksSELE 369
Cdd:cd05595  240 ggpSDAKEVMEHRFFLSINWQDVVQKKL--LPPFK-PQVT---------------SEVDTRYFD------------DEFT 289
                        330       340       350
                 ....*....|....*....|....*....|....
gi 564332436 370 GDTITLKPRPSADLTNSSAPSP-SHKVQRSVSAN 402
Cdd:cd05595  290 AQSITITPPDRYDSLDLLESDQrTHFPQFSYSAS 323
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
53-304 1.23e-50

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: 179.06  E-value: 1.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS----SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14194    7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgvSREDIEREVSILKEIQHPNVITLHEVYENKTDVILI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAEN-LLLDADM---NIKIADFGFSNEFTFGN 204
Cdd:cd14194   87 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKIIDFGLAHKIDFGN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFYMSTD--CENL 280
Cdd:cd14194  167 EFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFedEYFSNTSalAKDF 245
                        250       260
                 ....*....|....*....|....
gi 564332436 281 LKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14194  246 IRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
56-345 2.35e-50

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: 179.91  E-value: 2.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILT---GKEVAVKIIDKTQLNSSslQK----LFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd05584    1 LKVLGKGGYGKVFQVRKTTGsdkGKIFAMKVLKKASIVRN--QKdtahTKAERNILEAVKHPFIVDLHYAFQTGGKLYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLD- 207
Cdd:cd05584   79 LEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTh 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLIL 287
Cdd:cd05584  159 TFCGTIEYMAPEILT-RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKR 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 288 NPSKR-----GTLEQIMKDRWMNVGHEDDELKPYVEPlPdYKDPRRTELMVSM---GYTREEIQDS 345
Cdd:cd05584  238 NVSSRlgsgpGDAEEIKAHPFFRHINWDDLLAKKVEP-P-FKPLLQSEEDVSQfdsKFTKQTPVDS 301
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
59-300 2.64e-50

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: 178.24  E-value: 2.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKT--QLNSSSLQKL----FREVRIMK-VLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14181   18 IGRGVSSVVRRCVHRHTGQEFAVKIIEVTaeRLSPEQLEEVrsstLKEIHILRqVSGHPSIITLIDSYESSTFIFLVFDL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14181   98 MRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYD-----GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLK 282
Cdd:cd14181  178 TPGYLAPEILKCSMDEthpgyGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssPEWddRSSTVKDLIS 257
                        250
                 ....*....|....*...
gi 564332436 283 KFLILNPSKRGTLEQIMK 300
Cdd:cd14181  258 RLLVVDPEIRLTAEQALQ 275
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
59-304 4.77e-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: 176.65  E-value: 4.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKII------DKtqlnssslQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIkcrkakDR--------EDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL-LDADMN-IKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14103   73 AGGELFERVVDDDfELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLKVL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFqgkKYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY----MSTDCENLLKK 283
Cdd:cd14103  153 FGTPEFVAPEVV---NYEpiSYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEafddISDEAKDFISK 229
                        250       260
                 ....*....|....*....|.
gi 564332436 284 FLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14103  230 LLVKDPRKRMSAAQCLQHPWL 250
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
57-297 6.76e-50

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: 178.56  E-value: 6.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKdVILQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL-DTFCGSP 213
Cdd:cd05590   81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTtSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR- 292
Cdd:cd05590  161 DYIAPEILQEMLY-GPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRl 239

                 ....*
gi 564332436 293 GTLEQ 297
Cdd:cd05590  240 GSLTL 244
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
54-300 7.09e-50

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: 176.20  E-value: 7.09e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436    54 RLLKTIGKGNFAKVKLARHILTGK----EVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGDgkevEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   130 EYASGGEVFDYLVAHGR----MKEKearAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSnEFTFGN 204
Cdd:smart00221  81 EYMPGGDLLDYLRKNRPkelsLSDL---LSFaLQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS-RDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   205 KLDTFCGSP-PYA--APELFQGKKYdGPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCEN 279
Cdd:smart00221 157 DYYKVKGGKlPIRwmAPESLKEGKF-TSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLpKPPNCPPELYK 235
                          250       260
                   ....*....|....*....|.
gi 564332436   280 LLKKFLILNPSKRGTLEQIMK 300
Cdd:smart00221 236 LMLQCWAEDPEDRPTFSELVE 256
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
53-303 7.96e-50

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: 176.38  E-value: 7.96e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL----DADMNIKIADFGFSNefTFGNKLDT 208
Cdd:cd14184   82 KGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLAT--VVEGPLYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQ-NLKE-LRERVLRGK--YRIPFY--MSTDCENLLK 282
Cdd:cd14184  160 VCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRSEnNLQEdLFDQILLGKleFPSPYWdnITDSAKELIS 238
                        250       260
                 ....*....|....*....|.
gi 564332436 283 KFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14184  239 HMLQVNVEARYTAEQILSHPW 259
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
57-292 1.18e-49

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: 177.89  E-value: 1.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF---REVrIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHImaeRNV-LLKNVKHPFLVGLHYSFQTKDKLYFVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLvahgrMKEK---EARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLD 207
Cdd:cd05575   80 GGELFFHL-----QRERhfpEPRARFyaAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEgIEPSDTTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLIL 287
Cdd:cd05575  155 TFCGTPEYLAPEVLRKQPYDRT-VDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQK 233

                 ....*
gi 564332436 288 NPSKR 292
Cdd:cd05575  234 DRTKR 238
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
57-292 1.40e-49

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: 177.58  E-value: 1.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKV-LNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKdVVLEDDDVECTMIERRVLALaSQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFCGSP 213
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGeNKASTFCGTP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 214 PYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05592  161 DYIAPEILKGQKYNQ-SVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKR 238
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
54-300 4.22e-49

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 174.26  E-value: 4.22e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436    54 RLLKTIGKGNFAKVKLARHILTGK----EVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGGkkkvEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   130 EYASGGEVFDYLVAHGR---MKEKearAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK 205
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPklsLSDL---LSFaLQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   206 LDTFCGSPPYA--APELFQGKKYdGPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCENLL 281
Cdd:smart00219 158 YRKRGGKLPIRwmAPESLKEGKF-TSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLpQPPNCPPELYDLM 236
                          250
                   ....*....|....*....
gi 564332436   282 KKFLILNPSKRGTLEQIMK 300
Cdd:smart00219 237 LQCWAEDPEDRPTFSELVE 255
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
50-304 9.86e-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: 173.51  E-value: 9.86e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQ-KLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14117    5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEhQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEfTFGNKLDT 208
Cdd:cd14117   85 LEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH-APSLRRRT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd14117  164 MCGTLDYLPPEMIEGRTHD-EKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYH 242
                        250
                 ....*....|....*.
gi 564332436 289 PSKRGTLEQIMKDRWM 304
Cdd:cd14117  243 PSERLPLKGVMEHPWV 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
52-300 1.60e-48

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: 172.92  E-value: 1.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS---SSLQKLF--REVRI-MKVLNHPNIVKLFEVIETEKTL 125
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSkdgNDFQKLPqlREIDLhRRVSRHPNIITLHDVFETEVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYLVAHGRMKEKEARAK--FRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFGFSNefTF 202
Cdd:cd13993   81 YIVLEYCPNGDLFEAITENRIYVGKTELIKnvFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT--TE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPELF-----QGKKYDGPEVDVWSLGVILYTLVSGSLPF---------------DGQNLkelrerv 262
Cdd:cd13993  159 KISMDFGVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPWkiasesdpifydyylNSPNL------- 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 263 lrgkYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd13993  232 ----FDVILPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
52-300 1.69e-48

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: 172.60  E-value: 1.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAH-GR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNEFTFGNk 205
Cdd:cd08529   81 AENGDLHSLIKSQrGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGvakiLSDTTNFAQ- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 ldTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCENLLKKF 284
Cdd:cd08529  160 --TIVGTPYYLSPELCEDKPYN-EKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSC 236
                        250
                 ....*....|....*.
gi 564332436 285 LILNPSKRGTLEQIMK 300
Cdd:cd08529  237 LTKDYRQRPDTTELLR 252
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
53-304 8.71e-48

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: 170.81  E-value: 8.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-------MNIKIADFGFSNEfTFGNK 205
Cdd:cd14097   83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLSVQ-KYGLG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTF---CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN----LKELRERVLRGKYRIPFYMSTDCE 278
Cdd:cd14097  162 EDMLqetCGTPIYMAPEVISAHGYS-QQCDIWSIGVIMYMLLCGEPPFVAKSeeklFEEIRKGDLTFTQSVWQSVSDAAK 240
                        250       260
                 ....*....|....*....|....*.
gi 564332436 279 NLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14097  241 NVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
39-292 9.91e-48

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: 173.34  E-value: 9.91e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  39 NSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVLNHPNIVKLFE 117
Cdd:cd05593    3 DASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKeVIIAKDEVAHTLTESRVLKNTRHPFLTSLKY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 118 VIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS 197
Cdd:cd05593   83 SFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 NE-FTFGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTD 276
Cdd:cd05593  163 KEgITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSAD 241
                        250
                 ....*....|....*.
gi 564332436 277 CENLLKKFLILNPSKR 292
Cdd:cd05593  242 AKSLLSGLLIKDPNKR 257
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-304 1.36e-47

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: 171.38  E-value: 1.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLN--SSSLQKlfrEVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKgkESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGNKLD 207
Cdd:cd14168   89 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGDVMS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKK 283
Cdd:cd14168  169 TACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFdsPYWddISDSAKDFIRN 247
                        250       260
                 ....*....|....*....|.
gi 564332436 284 FLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14168  248 LMEKDPNKRYTCEQALRHPWI 268
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
57-298 2.29e-47

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: 169.26  E-value: 2.29e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLAR-HILTGK--EVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd00192    1 KKLGEGAFGEVYKGKlKGGDGKtvDVAVKTL-KEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKF---------RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSnEFTFGN 204
Cdd:cd00192   80 GGDLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLS-RDIYDD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPP----YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPF--YMSTDC 277
Cdd:cd00192  159 DYYRKKTGGKlpirWMAPESLKDGIFT-SKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKG-YRLPKpeNCPDEL 236
                        250       260
                 ....*....|....*....|.
gi 564332436 278 ENLLKKFLILNPSKRGTLEQI 298
Cdd:cd00192  237 YELMLSCWQLDPEDRPTFSEL 257
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
53-303 2.37e-47

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: 169.39  E-value: 2.37e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTI-GKGNFAKVKLARHILTGKEVAVKIIDKTQlnssslqKLFREVRI-MKVLNHPNIVKLFEVIET----EKTLY 126
Cdd:cd14089    2 YTISKQVlGLGINGKVLECFHKKTGEKFALKVLRDNP-------KARREVELhWRASGCPHIVRIIDVYENtyqgRKCLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMK--EKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFT 201
Cdd:cd14089   75 VVMECMEGGELFSRIQERADSAftEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGFAKETT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF---DGQNL-KELRERVLRGKYRIP----FYM 273
Cdd:cd14089  155 TKKSLQTPCYTPYYVAPEVLGPEKYD-KSCDMWSLGVIMYILLCGYPPFysnHGLAIsPGMKKRIRNGQYEFPnpewSNV 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 274 STDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14089  234 SEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
57-292 3.06e-47

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: 171.14  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKdVILQDDDVDCTMTEKRILALAaKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFdYLVAHGRmKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL-DTFCG 211
Cdd:cd05591   81 GDLM-FQIQRAR-KFDEPRARFyaAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTtTTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSK 291
Cdd:cd05591  159 TPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAK 237

                 .
gi 564332436 292 R 292
Cdd:cd05591  238 R 238
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
54-301 6.02e-47

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: 168.06  E-value: 6.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   54 RLLKTIGKGNFAKVKLAR----HILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTL-KEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  130 EYASGGEVFDYLVAHGR---MKEKearAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS----NEFT 201
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRkltLKDL---LSMaLQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSrdiyDDDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  202 FGNKLDTFCgSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYR--IPFYMSTDCE 278
Cdd:pfam07714 158 YRKRGGGKL-PIKWMAPESLKDGKFT-SKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDG-YRlpQPENCPDELY 234
                         250       260
                  ....*....|....*....|...
gi 564332436  279 NLLKKFLILNPSKRGTLEQIMKD 301
Cdd:pfam07714 235 DLMKQCWAYDPEDRPTFSELVED 257
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
53-306 6.93e-47

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: 168.64  E-value: 6.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS----SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14195    7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgvSREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAEN-LLLDADM---NIKIADFGFSNEFTFGN 204
Cdd:cd14195   87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIEAGN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI-PFYMSTDCE---NL 280
Cdd:cd14195  167 EFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFdEEYFSNTSElakDF 245
                        250       260
                 ....*....|....*....|....*.
gi 564332436 281 LKKFLILNPSKRGTLEQIMKDRWMNV 306
Cdd:cd14195  246 IRRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
53-303 2.08e-46

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: 167.74  E-value: 2.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI------ETEKTLY 126
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVtskgsaKYKGSIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASggevFDY--LVAHGRMKEKEARAK--FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT- 201
Cdd:cd07840   81 MVFEYMD----HDLtgLLDNPEVKFTESQIKcyMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTk 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 -----FGNKLDTFCgsppYAAPELFQG-KKYdGPEVDVWSLGVILYTLVSGSLPFDGQN--------------------- 254
Cdd:cd07840  157 ennadYTNRVITLW----YRPPELLLGaTRY-GPEVDMWSVGCILAELFTGKPIFQGKTeleqlekifelcgspteenwp 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332436 255 ------------LKELRERVLRGKYRipFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07840  232 gvsdlpwfenlkPKKPYKRRLREVFK--NVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
53-304 3.35e-46

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: 166.29  E-value: 3.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS----SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14196    7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHPNIITLHDVYENRTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAEN-LLLDADM---NIKIADFGFSNEFTFGN 204
Cdd:cd14196   87 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDGV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFYMSTD--CENL 280
Cdd:cd14196  167 EFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdeEFFSHTSelAKDF 245
                        250       260
                 ....*....|....*....|....
gi 564332436 281 LKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14196  246 IRKLLVKETRKRLTIQEALRHPWI 269
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
54-305 1.86e-45

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: 164.30  E-value: 1.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKEVAVKIIdktQLNSSSL--QKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKI---HVDGDEEfrKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSN--EFTFGNKlDT 208
Cdd:cd06623   81 MDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKvlENTLDQC-NT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLK---ELRERVLRGKyrIPFYMSTDCENLLKKF- 284
Cdd:cd06623  160 FVGTVTYMSPERIQGESYSYAA-DIWSLGLTLLECALGKFPFLPPGQPsffELMQAICDGP--PPSLPAEEFSPEFRDFi 236
                        250       260
                 ....*....|....*....|....
gi 564332436 285 ---LILNPSKRGTLEQIMKDRWMN 305
Cdd:cd06623  237 sacLQKDPKKRPSAAELLQHPFIK 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
59-302 1.87e-45

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: 164.41  E-value: 1.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGK-EVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14202   10 IGHGAFAVVFKGRHKEKHDlEVAVKCINKKNL-AKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA---------DMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14202   89 ADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYsggrksnpnNIRIKIADFGFARYLQNNMMAAT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP-FYMSTDCEnlLKKFLIl 287
Cdd:cd14202  169 LCGSPMYMAPEVIMSQHYDA-KADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPnIPRETSSH--LRQLLL- 244
                        250
                 ....*....|....*
gi 564332436 288 npskrGTLEQIMKDR 302
Cdd:cd14202  245 -----GLLQRNQKDR 254
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
53-301 2.48e-45

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: 165.94  E-value: 2.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLN---HPNIVKLFEVIETEKTLYLV 128
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDiIARDEVESLMCEKRIFETVNsarHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGG--------EVFDylvahgrmkekEARAKFRQ--IVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN 198
Cdd:cd05589   81 MEYAAGGdlmmhiheDVFS-----------EPRAVFYAacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 E-FTFGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDC 277
Cdd:cd05589  150 EgMGFGDRTSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEA 228
                        250       260
                 ....*....|....*....|....*
gi 564332436 278 ENLLKKFLILNPSKR-GTLEQIMKD 301
Cdd:cd05589  229 ISIMRRLLRKNPERRlGASERDAED 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
52-303 6.58e-45

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: 162.52  E-value: 6.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS---LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEAskeVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSneftfgNKLDT 208
Cdd:cd06625   81 MEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGAS------KRLQT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FC---------GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLP-FDGQNLKELRERVL-RGKYRIPFYMSTDC 277
Cdd:cd06625  155 ICsstgmksvtGTPYWMSPEVINGEGY-GRKADIWSVGCTVVEMLTTKPPwAEFEPMAAIFKIATqPTNPQLPPHVSEDA 233
                        250       260
                 ....*....|....*....|....*.
gi 564332436 278 ENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd06625  234 RDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
59-303 9.48e-45

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: 162.97  E-value: 9.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlqKLFREVRIMK-VLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14090   10 LGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRS--RVFREVETLHqCQGHPNILQLIEYFEDDERFYLVFEKMRGGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL---LDADMNIKIADFGFSNEFTFGN---------K 205
Cdd:cd14090   88 LSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKLSStsmtpvttpE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPEL-----FQGKKYDgPEVDVWSLGVILYTLVSGSLPFDG-----------------QNLkeLRERVL 263
Cdd:cd14090  168 LLTPVGSAEYMAPEVvdafvGEALSYD-KRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacqdcQEL--LFHSIQ 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564332436 264 RGKYRIP----FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14090  245 EGEYEFPekewSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
59-308 1.04e-44

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: 162.02  E-value: 1.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYlvaHGRMK---EKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF-GNKLDTFCGSP 213
Cdd:cd14187   95 LEL---HKRRKaltEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYdGERKKTLCGTP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFqGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRG 293
Cdd:cd14187  172 NYIAPEVL-SKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARP 250
                        250
                 ....*....|....*
gi 564332436 294 TLEQIMKDRWMNVGH 308
Cdd:cd14187  251 TINELLNDEFFTSGY 265
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
50-319 1.17e-44

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: 163.94  E-value: 1.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYL 127
Cdd:cd05619    4 IEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKdVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLFF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KL 206
Cdd:cd05619   84 VMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDaKT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLI 286
Cdd:cd05619  164 STFCGTPDYIAPEILLGQKY-NTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFV 242
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 287 LNPSKR----GTLEQIMKDRWMNVGH-EDDELKPYVEP 319
Cdd:cd05619  243 REPERRlgvrGDIRQHPFFREINWEAlEEREIEPPFKP 280
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-292 2.80e-44

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: 161.02  E-value: 2.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHIL---TGKEVAVKIIDKTqlnsSSLQKLFREVRIM---KVLNH----PNIVKLFEVIETEKTLYLV 128
Cdd:cd05583    2 LGTGAYGKVFLVRKVGghdAGKLYAMKVLKKA----TIVQKAKTAEHTMterQVLEAvrqsPFLVTLHYAFQTDAKLHLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd05583   78 LDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 --FCGSPPYAAPELFQGKKyDGPE--VDVWSLGVILYTLVSGSLPF--DGQ--NLKELRERVLRGKYRIPFYMSTDCENL 280
Cdd:cd05583  158 ysFCGTIEYMAPEVVRGGS-DGHDkaVDWWSLGVLTYELLTGASPFtvDGErnSQSEISKRILKSHPPIPKTFSAEAKDF 236
                        250
                 ....*....|..
gi 564332436 281 LKKFLILNPSKR 292
Cdd:cd05583  237 ILKLLEKDPKKR 248
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
56-292 3.08e-44

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: 162.56  E-value: 3.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVLNHPN-IVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKdVIIQDDDVECTMVEKRVLALSGKPPfLTQLHSCFQTMDRLYFVMEYVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLD-TFCGS 212
Cdd:cd05587   81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTrTFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05587  161 PDYIAPEIIAYQPY-GKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKR 239
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
57-300 6.53e-44

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: 159.32  E-value: 6.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS-SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPhQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-TFGNKLDTFCGSPP 214
Cdd:cd14189   87 SLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLePPEQRKKTICGTPN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELF--QGKkydGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd14189  167 YLAPEVLlrQGH---GPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDR 243

                 ....*...
gi 564332436 293 GTLEQIMK 300
Cdd:cd14189  244 LTLDQILE 251
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
57-300 7.86e-44

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: 159.41  E-value: 7.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS-SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPhQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTFCGSPP 214
Cdd:cd14188   87 SMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEpLEHRRRTICGTPN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGT 294
Cdd:cd14188  167 YLSPEVLN-KQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDRPS 245

                 ....*.
gi 564332436 295 LEQIMK 300
Cdd:cd14188  246 LDEIIR 251
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
53-305 9.30e-44

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: 159.39  E-value: 9.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14183    8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL----DADMNIKIADFGFSNefTFGNKLDT 208
Cdd:cd14183   87 KGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT--VVDGPLYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDG--QNLKELRERVLRGK--YRIPFY--MSTDCENLLK 282
Cdd:cd14183  165 VCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQvdFPSPYWdnVSDSAKELIT 243
                        250       260
                 ....*....|....*....|...
gi 564332436 283 KFLILNPSKRGTLEQIMKDRWMN 305
Cdd:cd14183  244 MMLQVDVDQRYSALQVLEHPWVN 266
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
52-300 1.28e-43

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: 159.00  E-value: 1.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNssslqKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14010    1 NYVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRP-----EVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS------NEFTFG-- 203
Cdd:cd14010   76 CTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeiLKELFGqf 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 ---------NKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVL-------RGKY 267
Cdd:cd14010  156 sdegnvnkvSKKQAKRGTPYYMAPELFQGGVHS-FASDLWALGCVLYEMFTGKPPFVAESFTELVEKILnedppppPPKV 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 268 RIPfyMSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14010  235 SSK--PSPDFKSLLKGLLEKDPAKRLSWDELVK 265
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
59-296 1.29e-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: 159.02  E-value: 1.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARH-ILTGKEVAVKIIDKTQLNSSSLQkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14201   14 VGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQIL-LGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLD---------ADMNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd14201   93 ADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYLQSNMMAAT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY---RIPFYMSTDCENLLKKFL 285
Cdd:cd14201  173 LCGSPMYMAPEVIMSQHYDA-KADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNlqpSIPRETSPYLADLLLGLL 251
                        250
                 ....*....|.
gi 564332436 286 ILNPSKRGTLE 296
Cdd:cd14201  252 QRNQKDRMDFE 262
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
57-292 1.39e-43

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: 160.49  E-value: 1.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKdVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFCGSP 213
Cdd:cd05620   81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGdNRASTFCGTP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 214 PYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05620  161 DYIAPEILQGLKYTF-SVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRR 238
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
57-292 1.42e-43

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: 160.64  E-value: 1.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHIL---TGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05582    1 KVLGQGSFGKVFLVRKITgpdAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF-GNKLDTFCGS 212
Cdd:cd05582   81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDhEKKAYSFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05582  161 VEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANR 239
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
52-292 1.59e-43

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: 161.74  E-value: 1.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS-SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05594   26 DFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCH-QKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDT 208
Cdd:cd05594  106 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd05594  186 FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKD 264

                 ....
gi 564332436 289 PSKR 292
Cdd:cd05594  265 PKQR 268
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
53-304 2.47e-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: 158.09  E-value: 2.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS----SSLQKLFREVRIMKVL----NHPNIVKLFEVIETEKT 124
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGE-VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM-NIKIADFGfSNEFTF 202
Cdd:cd14101   82 FLLVLERPQHCQdLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTgDIKLIDFG-SGATLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFdgqnlkELRERVLRGKYRIPFYMSTDCENLLK 282
Cdd:cd14101  161 DSMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPF------ERDTDILKAKPSFNKRVSNDCRSLIR 234
                        250       260
                 ....*....|....*....|..
gi 564332436 283 KFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14101  235 SCLAYNPSDRPSLEQILLHPWM 256
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
52-292 3.56e-43

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: 160.08  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHIL---TGKEVAVKIIDKTQL-NSSSLQKLFREVRimKVLNH----PNIVKLFEVIETEK 123
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALvQKAKTVEHTRTER--NVLEHvrqsPFLVTLHYAFQTDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG 203
Cdd:cd05614   79 KLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NKLDT--FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLK----ELRERVLRGKYRIPFYMSTDC 277
Cdd:cd05614  159 EKERTysFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKntqsEVSRRILKCDPPFPSFIGPVA 238
                        250
                 ....*....|....*
gi 564332436 278 ENLLKKFLILNPSKR 292
Cdd:cd05614  239 RDLLQKLLCKDPKKR 253
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
57-309 5.42e-43

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: 158.66  E-value: 5.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlqklfREVRIMKVLN-HPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ-----REIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGNK-LDTFCG 211
Cdd:cd14179   88 ELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQpLKTPCF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQ-------NLKELRERVLRGKYRIP----FYMSTDCENL 280
Cdd:cd14179  168 TLHYAAPELLNYNGYD-ESCDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQGDFSFEgeawKNVSQEAKDL 246
                        250       260
                 ....*....|....*....|....*....
gi 564332436 281 LKKFLILNPSKRGTLEQIMKDRWMNVGHE 309
Cdd:cd14179  247 IQGLLTVDPNKRIKMSGLRYNEWLQDGSQ 275
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
56-298 6.59e-43

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: 157.07  E-value: 6.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd13996   11 IELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSAS-EKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLV---AHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLD-ADMNIKIADFGF--------------- 196
Cdd:cd13996   90 TLRDWIDrrnSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLatsignqkrelnnln 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 197 SNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSgslPFDGQN-----LKELRervlRGKYRIPF 271
Cdd:cd13996  170 NNNNGNTSNNSVGIGTPLYASPEQLDGENYNEK-ADIYSLGIILFEMLH---PFKTAMerstiLTDLR----NGILPESF 241
                        250       260
                 ....*....|....*....|....*...
gi 564332436 272 YMSTDCE-NLLKKFLILNPSKRGTLEQI 298
Cdd:cd13996  242 KAKHPKEaDLIQSLLSKNPEERPSAEQL 269
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
52-304 7.07e-43

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: 156.62  E-value: 7.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLDTF-- 209
Cdd:cd06627   81 VENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLN-EVEKDENsv 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLP-FDGQNLKELrervlrgkYRI------PFymSTDCENLLK 282
Cdd:cd06627  160 VGTPYWMAPEVIEMSGV-TTASDIWSVGCTVIELLTGNPPyYDLQPMAAL--------FRIvqddhpPL--PENISPELR 228
                        250       260
                 ....*....|....*....|....*.
gi 564332436 283 KFLIL----NPSKRGTLEQIMKDRWM 304
Cdd:cd06627  229 DFLLQcfqkDPTLRPSAKELLKHPWL 254
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
53-303 7.64e-43

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: 156.24  E-value: 7.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKII-DKTQLNSSSLqklfREVRIMKVLN----HPNIVKLFEVIET--EKTL 125
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIkNDFRHPKAAL----REIKLLKHLNdvegHPNIVKLLDVFEHrgGNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYasGGEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADM-NIKIADFGFSNEFTf 202
Cdd:cd05118   77 CLVFEL--MGMNLYELIKDYPRGLPLDLIKSylYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLARSFT- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPE-LFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR--GKYripfymstDCEN 279
Cdd:cd05118  154 SPPYTPYVATRWYRAPEvLLGAKPYGSS-IDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRllGTP--------EALD 224
                        250       260
                 ....*....|....*....|....
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd05118  225 LLSKMLKYDPAKRITASQALAHPY 248
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
53-301 3.88e-42

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: 154.35  E-value: 3.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdktqLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVV----PVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDTFC 210
Cdd:cd06612   81 GAGSVSDIMKITNKtLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMaKRNTVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFdgQNLKELRERVLRG-----KYRIPFYMSTDCENLLKKFL 285
Cdd:cd06612  161 GTPFWMAPEVIQEIGYNN-KADIWSLGITAIEMAEGKPPY--SDIHPMRAIFMIPnkpppTLSDPEKWSPEFNDFVKKCL 237
                        250
                 ....*....|....*.
gi 564332436 286 ILNPSKRGTLEQIMKD 301
Cdd:cd06612  238 VKDPEERPSAIQLLQH 253
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
53-328 3.93e-42

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: 155.78  E-value: 3.93e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSS---SLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGG----EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNEFTf 202
Cdd:cd14094   85 EFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTF--CGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNlKELRERVLRGKYRIPFYM----STD 276
Cdd:cd14094  164 ESGLVAGgrVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQwshiSES 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564332436 277 CENLLKKFLILNPSKRGTLEQIMKDRWMnvghEDDELKPYVEPLPDYKDPRR 328
Cdd:cd14094  242 AKDLVRRMLMLDPAERITVYEALNHPWI----KERDRYAYRIHLPETVEQLR 289
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
53-318 4.48e-42

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: 154.71  E-value: 4.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDktqLNSSS--LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVID---LEEAEdeIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF-GNKLDTF 209
Cdd:cd06609   80 YCGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTStMSKRNTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPF-DGQNLKELRE-------RVLRGKYRIPFymstdcenll 281
Cdd:cd06609  159 VGTPFWMAPEVIKQSGYDE-KADIWSLGITAIELAKGEPPLsDLHPMRVLFLipknnppSLEGNKFSKPF---------- 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564332436 282 KKF----LILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVE 318
Cdd:cd06609  228 KDFvelcLNKDPKERPSAKELLKHKFIKKAKKTSYLTLLIE 268
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
53-304 5.45e-42

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: 155.11  E-value: 5.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL---------------NSSS---------LQKLFREVRIMKVLN 108
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgsKAAQgeqakplapLERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 109 HPNIVKLFEVIE--TEKTLYLVMEYASGGEVFDYLVAHgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD 186
Cdd:cd14200   82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVMEVPSDK-PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 187 MNIKIADFGFSNEFTfGN--KLDTFCGSPPYAAPELF--QGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERV 262
Cdd:cd14200  161 GHVKIADFGVSNQFE-GNdaLLSSTAGTPAFMAPETLsdSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564332436 263 LRGKYRIP--FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14200  240 KNKPVEFPeePEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
52-303 5.68e-42

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: 155.42  E-value: 5.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKII-------DKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVIETEKT 124
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklgerkeAKDGINFTAL----REIKLLQELKHPNIIGLLDVFGHKSN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGG-EV------FDYLVAHgrmkekeARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGfs 197
Cdd:cd07841   77 INLVFEFMETDlEKvikdksIVLTPAD-------IKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 neftfgnkLDTFCGSPP-----------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN-LKELR------ 259
Cdd:cd07841  148 --------LARSFGSPNrkmthqvvtrwYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSdIDQLGkifeal 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 260 ----ERVLRGKYRIPFYM-----------------STDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07841  220 gtptEENWPGVTSLPDYVefkpfpptplkqifpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-307 6.64e-42

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: 155.41  E-value: 6.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSslqklfREVRIMKVL-NHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRrMEANTQ------REVAALRLCqSHPNIVALHEVLHDQYHTYLVMELLRGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNEFTFGNK-LDTFCGS 212
Cdd:cd14180   88 LLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRpLQTPCFT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLK-------ELRERVLRGKYRIPF----YMSTDCENLL 281
Cdd:cd14180  168 LQYAAPELFSNQGYD-ESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEGeawkGVSEEAKDLV 246
                        250       260
                 ....*....|....*....|....*.
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWMNVG 307
Cdd:cd14180  247 RGLLTVDPAKRLKLSELRESDWLQGG 272
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
53-292 7.72e-42

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: 155.47  E-value: 7.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05574    3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMiKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL--VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADF--------------- 194
Cdd:cd05574   83 CPGGELFRLLqkQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvrk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 195 -GFSNEFTFGNKLDT--------------FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELR 259
Cdd:cd05574  163 sLRKGSRRSSVKSIEketfvaepsarsnsFVGTEEYIAPEVIKGDGH-GSAVDWWTLGILLYEMLYGTTPFKGSNRDETF 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564332436 260 ERVLRGKYRIPFY--MSTDCENLLKKFLILNPSKR 292
Cdd:cd05574  242 SNILKKELTFPESppVSSEAKDLIRKLLVKDPSKR 276
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
56-292 1.25e-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: 153.41  E-value: 1.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS-SSLQKLFREVRIMKVLNH-PNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAkNQVTNVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSP 213
Cdd:cd05611   81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNKKFVGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKyDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP----FYMSTDCENLLKKFLILNP 289
Cdd:cd05611  161 DYLAPETILGVG-DDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRLLCMDP 239

                 ...
gi 564332436 290 SKR 292
Cdd:cd05611  240 AKR 242
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
53-304 1.91e-41

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: 153.64  E-value: 1.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSslqklfREVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS------EEIEILlRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL-LDADMN---IKIADFGFSNEFTFGNK-L 206
Cdd:cd14175   77 MRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGlL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFD---GQNLKELRERVLRGKYRIPF----YMSTDCEN 279
Cdd:cd14175  157 MTPCYTANFVAPEVLKRQGYD-EGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGgnwnTVSDAAKD 235
                        250       260
                 ....*....|....*....|....*
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14175  236 LVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-300 2.23e-41

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: 152.27  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRM--KEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL-DTF 209
Cdd:cd08218   82 DGGDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELaRTC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCENLLKKFLILN 288
Cdd:cd08218  162 IGTPYYLSPEICENKPYNN-KSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRN 240
                        250
                 ....*....|..
gi 564332436 289 PSKRGTLEQIMK 300
Cdd:cd08218  241 PRDRPSINSILE 252
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
52-292 3.45e-41

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: 152.85  E-value: 3.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHIL---TGKEVAVKIIDK-TQLNSSSLQKLFREVRimKVLNH----PNIVKLFEVIETEK 123
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKaTIVQKAKTAEHTRTER--QVLEHirqsPFLVTLHYAFQTDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF- 202
Cdd:cd05613   79 KLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 -GNKLDTFCGSPPYAAPELFQGKK--YDgPEVDVWSLGVILYTLVSGSLPF--DGQN--LKELRERVLRGKYRIPFYMST 275
Cdd:cd05613  159 eNERAYSFCGTIEYMAPEIVRGGDsgHD-KAVDWWSLGVLMYELLTGASPFtvDGEKnsQAEISRRILKSEPPYPQEMSA 237
                        250
                 ....*....|....*..
gi 564332436 276 DCENLLKKFLILNPSKR 292
Cdd:cd05613  238 LAKDIIQRLLMKDPKKR 254
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-304 4.16e-41

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: 152.49  E-value: 4.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLL-KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlqKLFREVRIM-KVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14174    3 YRLTdELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRS--RVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNEFTFGN--- 204
Cdd:cd14174   81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFDLGSGVKLNSact 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 -----KLDTFCGSPPYAAPELF-----QGKKYDgPEVDVWSLGVILYTLVSGSLPFDG-----------------QNlkE 257
Cdd:cd14174  161 pittpELTTPCGSAEYMAPEVVevftdEATFYD-KRCDLWSLGVILYIMLSGYPPFVGhcgtdcgwdrgevcrvcQN--K 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 258 LRERVLRGKYRIP----FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14174  238 LFESIQEGKYEFPdkdwSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
52-292 4.76e-41

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: 153.62  E-value: 4.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVLNHPN-IVKLFEVIETEKTLYLVM 129
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKdVVIQDDDVECTMVEKRVLALSGKPPfLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF-GNKLDT 208
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWdGVTTKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd05616  161 FCGTPDYIAPEIIAYQPY-GKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKH 239

                 ....
gi 564332436 289 PSKR 292
Cdd:cd05616  240 PGKR 243
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
53-304 8.09e-41

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: 152.09  E-value: 8.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSslqklfREVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPS------EEIEILlRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL-LDADMN---IKIADFGFSNEFTFGNK-L 206
Cdd:cd14178   79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGlL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDG---QNLKELRERVLRGKYRIPF----YMSTDCEN 279
Cdd:cd14178  159 MTPCYTANFVAPEVLKRQGYDAA-CDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYALSGgnwdSISDAAKD 237
                        250       260
                 ....*....|....*....|....*
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14178  238 IVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
53-330 1.37e-40

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: 151.32  E-value: 1.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSslqklfREVRI-MKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPS------EEIEIlMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL-LDADMN---IKIADFGFSNEFTFGNK-L 206
Cdd:cd14177   80 MKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGlL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPF-DGQN--LKELRERVLRGKYRIPF----YMSTDCEN 279
Cdd:cd14177  160 LTPCYTANFVAPEVLMRQGYDAA-CDIWSLGVLLYTMLAGYTPFaNGPNdtPEEILLRIGSGKFSLSGgnwdTVSDAAKD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWmnVGHEDDelkpyvepLPDYKdPRRTE 330
Cdd:cd14177  239 LLSHMLHVDPHQRYTAEQVLKHSW--IACRDQ--------LPHYQ-LNRQD 278
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
50-304 2.50e-40

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: 150.12  E-value: 2.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS------------------------LQKLFREVRIMK 105
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAgfprrppprgaraapegctqprgpIERVYQEIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 106 VLNHPNIVKLFEVIE--TEKTLYLVMEYASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL 183
Cdd:cd14199   81 KLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 184 DADMNIKIADFGFSNEFTFGNK-LDTFCGSPPYAAPELFQG--KKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRE 260
Cdd:cd14199  160 GEDGHIKIADFGVSNEFEGSDAlLTNTVGTPAFMAPETLSEtrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 261 RVLRGKYRIPFY--MSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14199  240 KIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
37-304 6.02e-40

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 154.40  E-value: 6.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  37 GRNSATSADEQPHIgnYRLLKTIGKGNFAKVKLArhiLTGKEVAVKIIDKTQLNSSSLQKLF--REVRIMKVLNHPNIVK 114
Cdd:PTZ00267  55 GEEVPESNNPREHM--YVLTTLVGRNPTTAAFVA---TRGSDPKEKVVAKFVMLNDERQAAYarSELHCLAACDHFGIVK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 115 LFEVIETEKTLYLVMEYASGG----EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:PTZ00267 130 HFDDFKSDDKLLLIMEYGSGGdlnkQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIK 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFSNEFTFGNKLD---TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY 267
Cdd:PTZ00267 210 LGDFGFSKQYSDSVSLDvasSFCGTPYYLAPELWERKRYS-KKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKY 288
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 268 R-IPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:PTZ00267 289 DpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
52-300 7.41e-40

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: 148.18  E-value: 7.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL-VAHGRM-KEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFGFSNEFTFGNKLDT 208
Cdd:cd08225   81 CDGGDLMKRInRQRGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKLGDFGIARQLNDSMELAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FC-GSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCENLLKKFLI 286
Cdd:cd08225  161 TCvGTPYYLSPEICQNRPYNN-KTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApISPNFSRDLRSLISQLFK 239
                        250
                 ....*....|....
gi 564332436 287 LNPSKRGTLEQIMK 300
Cdd:cd08225  240 VSPRDRPSITSILK 253
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
56-305 9.49e-40

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: 149.69  E-value: 9.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnssslqkLFRE----VR----IMKVLNHPNIVKLFEVIETEKTLYL 127
Cdd:cd05599    6 LKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEM-------LEKEqvahVRaerdILAEADNPWVVKLYYSFQDEENLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQ-KFIvHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL 206
Cdd:cd05599   79 IMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKlGYI-HRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYM----STDCENLLK 282
Cdd:cd05599  158 YSTVGTPDYIAPEVFLQKGY-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPevpiSPEAKDLIE 236
                        250       260
                 ....*....|....*....|....*.
gi 564332436 283 KFLIlNPSKR---GTLEQIMKDRWMN 305
Cdd:cd05599  237 RLLC-DAEHRlgaNGVEEIKSHPFFK 261
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
57-303 9.54e-40

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: 147.83  E-value: 9.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEV-IETEKtLYLVMEYASGG 135
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVeVHREE-VYIFMEYCQEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDyLVAHGRMkEKEA--RAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS------NEFTFGNKLD 207
Cdd:cd06626   85 TLEE-LLRHGRI-LDEAviRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAvklknnTTTMAPGEVN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPE--VDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRG-KYRIP--FYMSTDCENLL 281
Cdd:cd06626  163 SLVGTPAYMAPEVITGNKGEGHGraADIWSLGCVVLEMATGKRPWsELDNEWAIMYHVGMGhKPPIPdsLQLSPEGKDFL 242
                        250       260
                 ....*....|....*....|..
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd06626  243 SRCLESDPKKRPTASELLDHPF 264
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
59-303 1.27e-39

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: 147.47  E-value: 1.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKtqlNSSSLQKLFREVRIMKVLN-HPNIVKLFEV-IETEKTLYLVMEYASGGE 136
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPK---PSTKLKDFLREYNISLELSvHPHIIKTYDVaFETEDYYVFAQEYAPYGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAEN-LLLDADMN-IKIADFGFSneFTFGNKLDTFCGSPP 214
Cdd:cd13987   78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDKDCRrVKLCDFGLT--RRVGSTVKRVSGTIP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYDG----PEVDVWSLGVILYTLVSGSLPFDGQNLKELR----ERVLRGK-YRIP-----FymSTDCENL 280
Cdd:cd13987  156 YTAPEVCEAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFyeefVRWQKRKnTAVPsqwrrF--TPKALRM 233
                        250       260
                 ....*....|....*....|....*.
gi 564332436 281 LKKFLILNPSKRGTLEQI---MKDRW 303
Cdd:cd13987  234 FKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
57-285 1.35e-39

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: 149.35  E-value: 1.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR--IMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERnvLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDTFCGSP 213
Cdd:cd05603   81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEETTSTFCGTP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332436 214 PYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd05603  161 EYLAPEVLRKEPYD-RTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLL 231
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
50-292 2.37e-39

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: 148.99  E-value: 2.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKLFREVRIMKVLNHPN-IVKLFEVIETEKTLYL 127
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKdVVIQDDDVECTMVEKRVLALQDKPPfLTQLHSCFQTVDRLYF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF-GNKL 206
Cdd:cd05615   89 VMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVeGVTT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLI 286
Cdd:cd05615  169 RTFCGTPDYIAPEIIAYQPY-GRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMT 247

                 ....*.
gi 564332436 287 LNPSKR 292
Cdd:cd05615  248 KHPAKR 253
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
48-317 2.39e-39

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: 149.01  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  48 PHI--GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR--IMKVLNHPNIVKLFEVIETEK 123
Cdd:cd05602    2 PHAkpSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERnvLLKNVKHPFLVGLHFSFQTTD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG 203
Cdd:cd05602   82 KLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 N-KLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLK 282
Cdd:cd05602  162 NgTTSTFCGTPEYLAPEVLHKQPYD-RTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLE 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564332436 283 KFLilnpskrgtleqiMKDRWMNVGHEDD--ELKPYV 317
Cdd:cd05602  241 GLL-------------QKDRTKRLGAKDDftEIKNHI 264
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
56-292 2.77e-39

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: 148.57  E-value: 2.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR--IMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERnvLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDTFCGS 212
Cdd:cd05604   81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEgISNSDTTTTFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05604  161 PEYLAPEVIRKQPYDN-TVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLR 239
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
53-304 3.06e-39

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: 148.63  E-value: 3.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSslqklfREVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL-LDADMN---IKIADFGFSNEFTFGNK-L 206
Cdd:cd14176   95 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGlL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDG---QNLKELRERVLRGKYRIP----FYMSTDCEN 279
Cdd:cd14176  175 MTPCYTANFVAPEVLERQGYDAA-CDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggywNSVSDTAKD 253
                        250       260
                 ....*....|....*....|....*
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14176  254 LVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
45-300 3.52e-39

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: 146.05  E-value: 3.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  45 DEQPHIGNYrllKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKT 124
Cdd:cd06648    4 DPRSDLDNF---VKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRREL--LFNEVVIMRDYQHPNIVEMYSSYLVGDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG- 203
Cdd:cd06648   79 LWVVMEFLEGGALTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEv 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLP-FDGQNLKELRErvLRG----KYRIPFYMSTDCE 278
Cdd:cd06648  158 PRRKSLVGTPYWMAPEVISRLPY-GTEVDIWSLGIMVIEMVDGEPPyFNEPPLQAMKR--IRDneppKLKNLHKVSPRLR 234
                        250       260
                 ....*....|....*....|..
gi 564332436 279 NLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd06648  235 SFLDRMLVRDPAQRATAAELLN 256
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
57-292 4.22e-39

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: 147.95  E-value: 4.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS-LQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEdIDWVQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKLDTFCGSP 213
Cdd:cd05588   81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGDTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFD--------GQNLKE-LRERVLRGKYRIPFYMSTDCENLLKKF 284
Cdd:cd05588  161 NYIAPEILRGEDYGF-SVDWWALGVLMFEMLAGRSPFDivgssdnpDQNTEDyLFQVILEKPIRIPRSLSVKAASVLKGF 239

                 ....*...
gi 564332436 285 LILNPSKR 292
Cdd:cd05588  240 LNKNPAER 247
MARK_C_like cd12121
C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
744-839 6.69e-39

C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases, and similar domains; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. In yeast, MARK/Par-1 homologs are called Kin1/2 kinases. Kin1 is a membrane-associated kinase that is involved in regulating cytokinesis and the cell surface. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213377  Cd Length: 96  Bit Score: 139.28  E-value: 6.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 744 RSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRISG 823
Cdd:cd12121    1 RSLRGPFSVATTSTKSPEEIMNEIKRVLRSNGIDYEEVGGYLLECKHGDSSGGEFVIFEIEICKLPRLGLNGIRFKRISG 80
                         90
                 ....*....|....*.
gi 564332436 824 TSMAFKNIASKIANEL 839
Cdd:cd12121   81 DSWQYKRLCKKILNEL 96
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
52-304 8.75e-39

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: 145.13  E-value: 8.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTI-GKGNFAKVKLARHILTGKEVAVKIIDKTQlnssslqKLFREVRI-MKVLNHPNIVKLFEVIET----EKTL 125
Cdd:cd14172    4 DYKLSKQVlGLGVNGKVLECFHRRTGQKCALKLLYDSP-------KARREVEHhWRASGGPHIVHILDVYENmhhgKRCL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYLVAHG--RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEF 200
Cdd:cd14172   77 LIIMECMEGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKET 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TFGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF---DGQNLKE-LRERVLRGKYRIP----FY 272
Cdd:cd14172  157 TVQNALQTPCYTPYYVAPEVLGPEKYD-KSCDMWSLGVIMYILLCGFPPFysnTGQAISPgMKRRIRMGQYGFPnpewAE 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564332436 273 MSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14172  236 VSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
53-304 1.12e-38

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: 144.78  E-value: 1.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFR-EVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14088    3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKR--DGRKVRKAAKnEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM---NIKIADFGFSneftfgnKLDT 208
Cdd:cd14088   81 ATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLknsKIVISDFHLA-------KLEN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 F-----CGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPF-------DGQNL-KELRERVLRGKYRI--PFY- 272
Cdd:cd14088  154 GlikepCGTPEYLAPEVVGRQRYGRP-VDCWAIGVIMYILLSGNPPFydeaeedDYENHdKNLFRKILAGDYEFdsPYWd 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 273 -MSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14088  233 dISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
52-298 1.16e-38

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: 144.72  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIID-KTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQiFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVfdylvahGRMKEKEARAK-----------FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG---- 195
Cdd:cd08224   81 LADAGDL-------SRLIKHFKKQKrlipertiwkyFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGlgrf 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 FSNEFTFGNKLdtfCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPF--DGQNLKELRERVLRGKYR-IP-F 271
Cdd:cd08224  154 FSSKTTAAHSL---VGTPYYMSPERIREQGYDFKS-DIWSLGCLLYEMAALQSPFygEKMNLYSLCKKIEKCEYPpLPaD 229
                        250       260
                 ....*....|....*....|....*..
gi 564332436 272 YMSTDCENLLKKFLILNPSKRGTLEQI 298
Cdd:cd08224  230 LYSQELRDLVAACIQPDPEKRPDISYV 256
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
47-285 1.16e-38

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: 147.52  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  47 QPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR-IMKVLNHPNIVKLFEVIETEKTL 125
Cdd:cd05596   22 RMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERdIMAHANSEWIVQLHYAFQDDKYL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK 205
Cdd:cd05596  102 YMVMDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 L--DTFCGSPPYAAPELFQ---GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTD 276
Cdd:cd05596  181 VrsDTAVGTPDYISPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKNSLQFpddvEISKD 260

                 ....*....
gi 564332436 277 CENLLKKFL 285
Cdd:cd05596  261 AKSLICAFL 269
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
39-292 1.22e-38

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: 147.87  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  39 NSATSADEQPHIG--NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS-LQKLFREVRIM-KVLNHPNIVK 114
Cdd:cd05618    6 NSRESGKASSSLGlqDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEdIDWVQTEKHVFeQASNHPFLVG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 115 LFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADF 194
Cdd:cd05618   86 LHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 195 GFSNE-FTFGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFD--------GQNLKE-LRERVLR 264
Cdd:cd05618  166 GMCKEgLRPGDTTSTFCGTPNYIAPEILRGEDY-GFSVDWWALGVLMFEMMAGRSPFDivgssdnpDQNTEDyLFQVILE 244
                        250       260
                 ....*....|....*....|....*...
gi 564332436 265 GKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05618  245 KQIRIPRSLSVKAASVLKSFLNKDPKER 272
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
52-299 1.43e-38

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: 144.35  E-value: 1.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEI-RLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL-VAHGRM-KEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNEFTFGNk 205
Cdd:cd08219   80 CDGGDLMQKIkLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLTSPGAYAC- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 ldTFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTDCENLLKKF 284
Cdd:cd08219  159 --TYVGTPYYVPPEIWENMPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQM 235
                        250
                 ....*....|....*
gi 564332436 285 LILNPSKRGTLEQIM 299
Cdd:cd08219  236 FKRNPRSRPSATTIL 250
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
57-299 1.64e-38

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: 144.08  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVK---IIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSP 213
Cdd:cd06632   86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFKGSP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELF--QGKKYDGPeVDVWSLGVILYTLVSGSLPFdGQ-----------NLKELRErvlrgkyrIPFYMSTDCENL 280
Cdd:cd06632  166 YWMAPEVImqKNSGYGLA-VDIWSLGCTVLEMATGKPPW-SQyegvaaifkigNSGELPP--------IPDHLSPDAKDF 235
                        250
                 ....*....|....*....
gi 564332436 281 LKKFLILNPSKRGTLEQIM 299
Cdd:cd06632  236 IRLCLQRDPEDRPTASQLL 254
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
57-303 1.86e-38

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: 144.09  E-value: 1.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASgGE 136
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH-GD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSN---EFTFGNkldT 208
Cdd:cd14082   88 MLEMILSSekGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARiigEKSFRR---S 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQnlKELRERVLRGKYRIP----FYMSTDCENLLKKF 284
Cdd:cd14082  165 VVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNED--EDINDQIQNAAFMYPpnpwKEISPDAIDLINNL 241
                        250
                 ....*....|....*....
gi 564332436 285 LILNPSKRGTLEQIMKDRW 303
Cdd:cd14082  242 LQVKMRKRYSVDKSLSHPW 260
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
52-303 2.34e-38

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: 144.78  E-value: 2.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLN-HPNIVKLFEVIETEKTLYLVME 130
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGG--EVfdylVAHGR--MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNEftf 202
Cdd:cd07832   81 YMLSSlsEV----LRDEErpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGlarlFSEE--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTF-CGSPPYAAPELFQGK-KYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR-----------GKYRI 269
Cdd:cd07832  154 DPRLYSHqVATRWYRAPELLYGSrKYD-EGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRtlgtpnektwpELTSL 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564332436 270 PFY---------------MSTDCE----NLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07832  233 PDYnkitfpeskgirleeIFPDCSpeaiDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
50-292 2.40e-38

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: 146.70  E-value: 2.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIM-KVLNHPNIVKLFEVIETEKTLYL 127
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVhDDEDIDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-FTFGNKL 206
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEgLGPGDTT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFD------GQNLKE-LRERVLRGKYRIPFYMSTDCEN 279
Cdd:cd05617  174 STFCGTPNYIAPEILRGEEY-GFSVDWWALGVLMFEMMAGRSPFDiitdnpDMNTEDyLFQVILEKPIRIPRFLSVKASH 252
                        250
                 ....*....|...
gi 564332436 280 LLKKFLILNPSKR 292
Cdd:cd05617  253 VLKGFLNKDPKER 265
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-304 2.72e-38

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: 144.40  E-value: 2.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTI-GKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlqKLFREVRIM-KVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14173    3 YQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRS--RVFREVEMLyQCQGHRNVLELIEFFEEEDKFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNI---KIADFGFSNEFTFGN--- 204
Cdd:cd14173   81 KMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSGIKLNSdcs 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 -----KLDTFCGSPPYAAPELF-----QGKKYDgPEVDVWSLGVILYTLVSGSLPFDG-----------------QNLke 257
Cdd:cd14173  161 pistpELLTPCGSAEYMAPEVVeafneEASIYD-KRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwdrgeacpacQNM-- 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 258 LRERVLRGKYRIP----FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14173  238 LFESIQEGKYEFPekdwAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
53-304 4.25e-38

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: 143.77  E-value: 4.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDktqLNSSS--LQKLFREVRIMKVLNH---PNIVKLFEVIETEKTLYL 127
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLN---LDTDDddVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAhGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KL 206
Cdd:cd06917   80 IMDYCEGGSIRTLMRA-GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSsKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELF-QGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLkeLRERVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd06917  159 STFVGTPYWMAPEVItEGKYYD-TKADIWSLGITTYEMATGNPPYSDVDA--LRAVMLIPKSKPPRLEGNGYSPLLKEFV 235
                        250       260
                 ....*....|....*....|...
gi 564332436 286 IL----NPSKRGTLEQIMKDRWM 304
Cdd:cd06917  236 AAcldeEPKDRLSADELLKSKWI 258
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
59-292 4.60e-38

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: 144.64  E-value: 4.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS-SSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSrSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-EFTFGNKLDTFCGSPPYA 216
Cdd:cd05585   82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKlNMKDDDKTNTFCGTPEYL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 217 APELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05585  162 APELLLGHGYT-KAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKR 236
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
52-306 5.83e-38

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: 143.34  E-value: 5.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdktQLNSSS-LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd06611    6 IWEIIGELGDGAFGKVYKAQHKETGLFAAAKII---QIESEEeLEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS--NEFTFgNKLD 207
Cdd:cd06611   83 FCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSakNKSTL-QKRD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPEL-----FQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRG---KYRIPFYMSTDCEN 279
Cdd:cd06611  162 TFIGTPYWMAPEVvacetFKDNPYDY-KADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSeppTLDQPSKWSSSFND 240
                        250       260
                 ....*....|....*....|....*..
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWMNV 306
Cdd:cd06611  241 FLKSCLVKDPDDRPTAAELLKHPFVSD 267
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
59-304 5.90e-38

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: 142.75  E-value: 5.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQ--NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN--IKIADFGFSNEFTFGNKLDTFCGSPPY 215
Cdd:cd14190   90 ERIVDEDyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhqVKIIDFGLARRYNPREKLKVNFGTPEF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PF-YMSTDCENLLKKFLILNPSK 291
Cdd:cd14190  170 LSPEVVNYDQVSFP-TDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFdeeTFeHVSDEAKDFVSNLIIKERSA 248
                        250
                 ....*....|...
gi 564332436 292 RGTLEQIMKDRWM 304
Cdd:cd14190  249 RMSATQCLKHPWL 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
53-300 7.55e-38

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: 142.50  E-value: 7.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSsLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTS-MDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFD---YLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-NEFTFGN---- 204
Cdd:cd06610   82 SGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSaSLATGGDrtrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPE-LFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQ------------NLKELRERVLRGKYRIPF 271
Cdd:cd06610  162 VRKTFVGTPCWMAPEvMEQVRGYDF-KADIWSFGITAIELATGAAPYSKYppmkvlmltlqnDPPSLETGADYKKYSKSF 240
                        250       260
                 ....*....|....*....|....*....
gi 564332436 272 ymstdcENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd06610  241 ------RKMISLCLQKDPSKRPTAEELLK 263
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
53-301 7.99e-38

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: 142.84  E-value: 7.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIidkTQLNSS-SLQK-------LFREVRIMKVLNHPNIVKLFEVIETEK- 123
Cdd:cd13990    2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKI---HQLNKDwSEEKkqnyikhALREYEIHKSLDHPRIVKLYDVFEIDTd 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYC--HQKFIVHRDLKAENLLLDADM---NIKIADFGFSN 198
Cdd:cd13990   79 SFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNvsgEIKITDFGLSK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFTFGNKLDT-------FCGSPPYAAPELFQGKKyDGP----EVDVWSLGVILYTLVSGSLPFdGQNL---KELRERVLR 264
Cdd:cd13990  159 IMDDESYNSDgmeltsqGAGTYWYLPPECFVVGK-TPPkissKVDVWSVGVIFYQMLYGRKPF-GHNQsqeAILEENTIL 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564332436 265 GKYRIPF----YMSTDCENLLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd13990  237 KATEVEFpskpVVSSEAKDFIRRCLTYRKEDRPDVLQLAND 277
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
59-304 1.32e-37

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: 141.75  E-value: 1.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS---SSLQK-----LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSdraDSRQKtvvdaLKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS--NEFTFGNKLDT 208
Cdd:cd06629   89 YVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISkkSDDIYGNNGAT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 -FCGSPPYAAPELF--QGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLL 281
Cdd:cd06629  169 sMQGSVFWMAPEVIhsQGQGY-SAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVpedvNLSPEALDFL 247
                        250       260
                 ....*....|....*....|...
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd06629  248 NACFAIDPRDRPTAAELLSHPFL 270
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
53-300 1.52e-37

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: 141.60  E-value: 1.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTFCG 211
Cdd:cd06647   87 AGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENLL 281
Cdd:cd06647  166 TPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSAIFRDFL 237
                        250
                 ....*....|....*....
gi 564332436 282 KKFLILNPSKRGTLEQIMK 300
Cdd:cd06647  238 NRCLEMDVEKRGSAKELLQ 256
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
52-294 1.82e-37

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: 141.77  E-value: 1.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLN-SSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLIlRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFT---- 201
Cdd:cd05609   81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglmSLTTnlye 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 ---------FGNKldTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF- 271
Cdd:cd05609  161 ghiekdtreFLDK--QVCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEg 237
                        250       260
                 ....*....|....*....|....*.
gi 564332436 272 --YMSTDCENLLKKFLILNPSKR-GT 294
Cdd:cd05609  238 ddALPDDAQDLITRLLQQNPLERlGT 263
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
57-304 1.99e-37

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: 141.61  E-value: 1.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLN-HPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd14197   15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAHGR--MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM---NIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd14197   95 EIFNQCVADREeaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKNSEELREIM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRipfYMSTDCENL-------L 281
Cdd:cd14197  175 GTPEYVAPEILS---YEpiSTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVS---YSEEEFEHLsesaidfI 248
                        250       260
                 ....*....|....*....|...
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14197  249 KTLLIKKPENRATAEDCLKHPWL 271
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
53-304 3.92e-37

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: 140.50  E-value: 3.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQklfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14113    9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVT---HELGVLQSLQHPQLVGLLDTFETPTSYILVLEMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14113   86 DQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNTTYYIHQL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP--FY--MSTDCENLLKKFL 285
Cdd:cd14113  166 LGSPEFAAPEIILGNPVSLTS-DLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddYFkgVSQKAKDFVCFLL 244
                        250
                 ....*....|....*....
gi 564332436 286 ILNPSKRGTLEQIMKDRWM 304
Cdd:cd14113  245 QMDPAKRPSAALCLQEQWL 263
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
51-262 3.95e-37

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 147.63  E-value: 3.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQL-NSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:NF033483   7 GRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL-RPDLaRDPEFVARFrREAQSAASLSHPNIVSVYDVGEDGGIPYIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNE-FTFG 203
Cdd:NF033483  86 MEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTtMTQT 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 204 NKLdtfCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-----LKELRERV 262
Cdd:NF033483 166 NSV---LGTVHYLSPEQARGGTVD-ARSDIYSLGIVLYEMLTGRPPFDGDSpvsvaYKHVQEDP 225
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
59-292 4.07e-37

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: 142.32  E-value: 4.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMK---VLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIvAKKEVAHTIGERNILVrtaLDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL-DTFCGSP 213
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTtNTFCGTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF-YMSTDCENLLKKFLILNPSKR 292
Cdd:cd05586  161 EYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHR 240
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
59-300 4.16e-37

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: 139.88  E-value: 4.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARhiLTGKEVAVKIIDktqlnSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14058    1 VGRGSFGVVCKAR--WRNQIVAVKIIE-----SESEKKAFeVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLvaHGRMKEKE-----ARAKFRQIVSAVQYCHQ---KFIVHRDLKAENLLL-DADMNIKIADFG----FSNEFTfGN 204
Cdd:cd14058   74 YNVL--HGKEPKPIytaahAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLtNGGTVLKICDFGtacdISTHMT-NN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KldtfcGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRE--RVLRGKyRIPfyMSTDC----E 278
Cdd:cd14058  151 K-----GSAAWMAPEVFEGSKYS-EKCDVFSWGIILWEVITRRKPFDHIGGPAFRImwAVHNGE-RPP--LIKNCpkpiE 221
                        250       260
                 ....*....|....*....|..
gi 564332436 279 NLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14058  222 SLMTRCWSKDPEKRPSMKEIVK 243
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
53-304 5.77e-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: 139.70  E-value: 5.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDK---TQLNSSSLQKLFREVRIMKVLNHP--NIVKLFEVIETEKTLYL 127
Cdd:cd14102    2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKervTEWGTLNGVMVPLEIVLLKKVGSGfrGVIKLLDWYERPDGFLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYAS-GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA-DMNIKIADFGfSNEFTFGNK 205
Cdd:cd14102   82 VMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLrTGELKLIDFG-SGALLKDTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFdgqnlkELRERVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd14102  161 YTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPF------EQDEEILRGRLYFRRRVSPECQQLIKWCL 234
                        250
                 ....*....|....*....
gi 564332436 286 ILNPSKRGTLEQIMKDRWM 304
Cdd:cd14102  235 SLRPSDRPTLEQIFDHPWM 253
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
51-254 6.68e-37

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: 140.53  E-value: 6.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YAsGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK--LD 207
Cdd:cd07833   81 YV-ERTLLELLEASpGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPAspLT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd07833  160 DYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDS 206
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
59-292 7.85e-37

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: 139.97  E-value: 7.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMaLNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPY 215
Cdd:cd05577   81 KYHIYNVGTRGFSEARAIFyaAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTHGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKK-YDGPeVDVWSLGVILYTLVSGSLPFDGQNLK----ELRERVLRGKYRIPFYMSTDCENLLKKFLILNPS 290
Cdd:cd05577  161 MAPEVLQKEVaYDFS-VDWFALGCMLYEMIAGRSPFRQRKEKvdkeELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPE 239

                 ..
gi 564332436 291 KR 292
Cdd:cd05577  240 RR 241
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
57-304 1.03e-36

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: 139.29  E-value: 1.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd14198   14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAkSNPRVVNLHEVYETTSEIILILEYAAGG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVA--HGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM---NIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd14198   94 EIFNLCVPdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKIGHACELREIM 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKE--LRERVLRGKYRIPFY--MSTDCENLLKKF 284
Cdd:cd14198  174 GTPEYLAPEILN---YDpiTTATDMWNIGVIAYMLLTHESPFVGEDNQEtfLNISQVNVDYSEETFssVSQLATDFIQKL 250
                        250       260
                 ....*....|....*....|
gi 564332436 285 LILNPSKRGTLEQIMKDRWM 304
Cdd:cd14198  251 LVKNPEKRPTAEICLSHSWL 270
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
53-302 1.10e-36

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: 138.98  E-value: 1.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKII---DKTQLnsSSLQKlfrEVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd06613    2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIklePGDDF--EIIQQ---EISMLKECRHPNIVAYFGSYLRRDKLWIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDT 208
Cdd:cd06613   77 EYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATiAKRKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKK---YDGpEVDVWSLGVILYTLVSGSLP-FDgqnLKELRERVLRGKYRIPFYMSTDCE------ 278
Cdd:cd06613  157 FIGTPYWMAPEVAAVERkggYDG-KCDIWALGITAIELAELQPPmFD---LHPMRALFLIPKSNFDPPKLKDKEkwspdf 232
                        250       260
                 ....*....|....*....|....*
gi 564332436 279 -NLLKKFLILNPSKRGTLEQIMKDR 302
Cdd:cd06613  233 hDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
57-304 1.26e-36

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: 138.94  E-value: 1.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVK--NEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL--DADMNIKIADFGFSNEFTFGNKLDTFCGSP 213
Cdd:cd14192   88 LFDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLARRYKPREKLKVNFGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKFLILNP 289
Cdd:cd14192  168 EFLAPEVVNYDFVSFP-TDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAeafeNLSEEAKDFISRLLVKEK 246
                        250
                 ....*....|....*
gi 564332436 290 SKRGTLEQIMKDRWM 304
Cdd:cd14192  247 SCRMSATQCLKHEWL 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
53-304 1.57e-36

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: 138.49  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14114    4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPH--ESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVA-HGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA--DMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14114   82 SGGELFERIAAeHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTkrSNEVKLIDFGLATHLDPKESVKVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKFL 285
Cdd:cd14114  162 TGTAEFAAPEIVEREPV-GFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDsafsGISEEAKDFIRKLL 240
                        250
                 ....*....|....*....
gi 564332436 286 ILNPSKRGTLEQIMKDRWM 304
Cdd:cd14114  241 LADPNKRMTIHQALEHPWL 259
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
33-325 2.12e-36

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 140.50  E-value: 2.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  33 NMLRGRNSATSADEQPHIGN------YRLLKTIGKGNFAKVKLARHILTG-KEVAVKIIDKTQL-NSSSLQKLFREVRIM 104
Cdd:PTZ00426   6 NLQLHKKKDSDSTKEPKRKNkmkyedFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIiKQKQVDHVFSERKIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 105 KVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLD 184
Cdd:PTZ00426  86 NYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 185 ADMNIKIADFGFSNefTFGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR 264
Cdd:PTZ00426 166 KDGFIKMTDFGFAK--VVDTRTYTLCGTPEYIAPEILLNVGH-GKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILE 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332436 265 GKYRIPFYMSTDCENLLKKFLILNPSKR-GTLE---QIMKDR-------WMNVGHEDDELkPYVeplPDYKD 325
Cdd:PTZ00426 243 GIIYFPKFLDNNCKHLMKKLLSHDLTKRyGNLKkgaQNVKEHpwfgnidWVSLLHKNVEV-PYK---PKYKN 310
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-301 2.78e-36

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: 137.94  E-value: 2.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILT--GKEVAV-KIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKAtaDEELKVlKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFD----YLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMnIKIADFGFSNEFTFGNK 205
Cdd:cd08222   82 EYCEGGDLDDkiseYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILMGTSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 L-DTFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCENLLKK 283
Cdd:cd08222  161 LaTTFTGTPYYMSPEVLKHEGYNS-KSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSR 239
                        250
                 ....*....|....*...
gi 564332436 284 FLILNPSKRGTLEQIMKD 301
Cdd:cd08222  240 MLNKDPALRPSAAEILKI 257
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
53-303 2.82e-36

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: 138.58  E-value: 2.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKII----DKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIrletEDEGVPSTAI----REISLLKELNHPNIVRLLDVVHSENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASggevFD---YLVAHGRMKEKEARAK--FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF--- 200
Cdd:cd07835   77 FEFLD----LDlkkYMDSSPLTGLDPPLIKsyLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFgvp 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 --TFGNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-----QNLKELR------ERVLRGKY 267
Cdd:cd07835  153 vrTYTHEVVTLW----YRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGdseidQLFRIFRtlgtpdEDVWPGVT 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564332436 268 RIPFYMST------------------DCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07835  229 SLPDYKPTfpkwarqdlskvvpsldeDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
57-304 3.02e-36

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: 138.75  E-value: 3.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKI-IDKtqlnssslQKLFREVRI-MKVLNHPNIVKLFEVIETE----------KT 124
Cdd:cd14171   12 QKLGTGISGPVRVCVKKSTGERFALKIlLDR--------PKARTEVRLhMMCSGHPNIVQIYDVYANSvqfpgessprAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEfT 201
Cdd:cd14171   84 LLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAKV-D 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNkLDTFCGSPPYAAPELFQGKKYDGPE----------------VDVWSLGVILYTLVSGSLPF-----DGQNLKELRE 260
Cdd:cd14171  163 QGD-LMTPQFTPYYVAPQVLEAQRRHRKErsgiptsptpytydksCDMWSLGVIIYIMLCGYPPFysehpSRTITKDMKR 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 261 RVLRGKYRIP----FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14171  242 KIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-304 3.60e-36

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: 137.57  E-value: 3.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVMEY 131
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHG--RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL-DT 208
Cdd:cd08223   82 CEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMaTT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCENLLKKFLIL 287
Cdd:cd08223  162 LIGTPYYMSPELFSNKPYN-HKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAMLHQ 240
                        250
                 ....*....|....*..
gi 564332436 288 NPSKRGTLEQIMKDRWM 304
Cdd:cd08223  241 DPEKRPSVKRILRQPYI 257
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
52-300 5.73e-36

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: 136.74  E-value: 5.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRI-MKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAhAALGQHPNIVRYYSSWEEGGHLYIQME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGG---EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGnkLD 207
Cdd:cd13997   81 LCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETS--GD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGS-LPFDGQNLKELRErvlrGKYRIPF--YMSTDCENLLKKF 284
Cdd:cd13997  159 VEEGDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEpLPRNGQQWQQLRQ----GKLPLPPglVLSQELTRLLKVM 234
                        250
                 ....*....|....*.
gi 564332436 285 LILNPSKRGTLEQIMK 300
Cdd:cd13997  235 LDPDPTRRPTADQLLA 250
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
52-285 6.44e-36

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: 140.91  E-value: 6.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR-IMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05622   74 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVME 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN--KLDT 208
Cdd:cd05622  154 YMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvRCDT 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQ---GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY----MSTDCENLL 281
Cdd:cd05622  233 AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPddndISKEAKNLI 312

                 ....
gi 564332436 282 KKFL 285
Cdd:cd05622  313 CAFL 316
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
56-305 9.08e-36

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: 136.32  E-value: 9.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIdktQLNS-SSLQK-LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd06605    6 LGELGEGNGGVVSKVRHRPSGQIMAVKVI---RLEIdEALQKqILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLDTFCGS 212
Cdd:cd06605   83 GGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV-DSLAKTFVGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLK------ELRERVLRGKY-RIPFYM-STDCENLLKKF 284
Cdd:cd06605  162 RSYMAPERISGGKYT-VKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEPPpLLPSGKfSPDFQDFVSQC 240
                        250       260
                 ....*....|....*....|.
gi 564332436 285 LILNPSKRGTLEQIMKDRWMN 305
Cdd:cd06605  241 LQKDPTERPSYKELMEHPFIK 261
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
57-300 9.61e-36

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: 138.21  E-value: 9.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR-IMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd05601    7 NVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERdIMAKANSPWITKLQYAFQDSENLYLVMEYHPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLDTF---CG 211
Cdd:cd05601   87 DLLSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLS-SDKTVTSkmpVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQ-----GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY----MSTDCENLLK 282
Cdd:cd05601  166 TPDYIAPEVLTsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPedpkVSESAVDLIK 245
                        250
                 ....*....|....*...
gi 564332436 283 KfLILNPSKRGTLEQIMK 300
Cdd:cd05601  246 G-LLTDAKERLGYEGLCC 262
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-300 1.28e-35

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: 135.63  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd08221    2 YIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGR--MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL-DTF 209
Cdd:cd08221   82 NGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMaESI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR--IPFYmSTDCENLLKKFLIL 287
Cdd:cd08221  162 VGTPYYMSPELVQGVKYN-FKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEdiDEQY-SEEIIQLVHDCLHQ 239
                        250
                 ....*....|...
gi 564332436 288 NPSKRGTLEQIMK 300
Cdd:cd08221  240 DPEDRPTAEELLE 252
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
53-304 1.33e-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: 136.51  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNS-SSLQKLfREVR-IMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-KKKFYSwEECMNL-REVKsLRKLNEHPNIVKLKEVFRENDELYFVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGgEVFDYLVAHGRMK--EKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEftfgnkldt 208
Cdd:cd07830   79 YMEG-NLYQLMKDRKGKPfsESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLARE--------- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPP---------YAAPE-LFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNlkELRE-----RVL---------R 264
Cdd:cd07830  149 IRSRPPytdyvstrwYRAPEiLLRSTSYSSP-VDIWALGCIMAELYTLRPLFPGSS--EIDQlykicSVLgtptkqdwpE 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 265 GK-------YRIPFYMST-----------DCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd07830  226 GYklasklgFRFPQFAPTslhqlipnaspEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
53-304 1.41e-35

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: 135.48  E-value: 1.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS----SSLQKLFREVRIMKVLNH--PNIVKLFEVIETEKTLY 126
Cdd:cd14100    2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEwgelPNGTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASG-GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM-NIKIADFGfSNEFTFGN 204
Cdd:cd14100   82 LVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTgELKLIDFG-SGALLKDT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFdgqnlkELRERVLRGKYRIPFYMSTDCENLLKKF 284
Cdd:cd14100  161 VYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPF------EHDEEIIRGQVFFRQRVSSECQHLIKWC 234
                        250       260
                 ....*....|....*....|
gi 564332436 285 LILNPSKRGTLEQIMKDRWM 304
Cdd:cd14100  235 LALRPSDRPSFEDIQNHPWM 254
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
35-300 3.00e-35

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: 138.24  E-value: 3.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  35 LRGRNSatsadeQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIidktqLNSSSLQKLfREVR-------IMKVL 107
Cdd:cd05600    1 LRKRRT------RLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKI-----MKKKVLFKL-NEVNhvlterdILTTT 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 108 NHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM 187
Cdd:cd05600   69 NSPWLVKLLYAFQDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 188 NIKIADFGFSNEF--------------------------------------TFGNKLDTFCGSPPYAAPELFQGKKYDgP 229
Cdd:cd05600  149 HIKLTDFGLASGTlspkkiesmkirleevkntafleltakerrniyramrkEDQNYANSVVGSPDYMAPEVLRGEGYD-L 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 230 EVDVWSLGVILYTLVSGSLPFDG-------QNLKELRERVLRGKY---RIPFYMSTDCENLLKKfLILNPSKR-GTLEQI 298
Cdd:cd05600  228 TVDYWSLGCILFECLVGFPPFSGstpnetwANLYHWKKTLQRPVYtdpDLEFNLSDEAWDLITK-LITDPQDRlQSPEQI 306

                 ..
gi 564332436 299 MK 300
Cdd:cd05600  307 KN 308
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
53-317 1.17e-34

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: 134.47  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTFCG 211
Cdd:cd06654  100 AGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMVG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENLL 281
Cdd:cd06654  179 TPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSAIFRDFL 250
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYV 317
Cdd:cd06654  251 NRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLI 286
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
55-300 1.20e-34

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: 132.86  E-value: 1.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLArhILTGKEVAVKIIDKtqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05039   10 LGELIGKGEFGDVMLG--DYRGQKVAVKCLKD---DSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGR-MKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGnkLDTfcGS 212
Cdd:cd05039   85 GSLVDYLRSRGRaVITRKDQLGFaLDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSN--QDG--GK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRI--P-------FYMSTDCENl 280
Cdd:cd05039  161 LPikWTAPEALREKKFST-KSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPHVEKG-YRMeaPegcppevYKVMKNCWE- 237
                        250       260
                 ....*....|....*....|
gi 564332436 281 lkkfliLNPSKRGTLEQIMK 300
Cdd:cd05039  238 ------LDPAKRPTFKQLRE 251
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
53-303 1.70e-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: 132.71  E-value: 1.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFI---PLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL--DADMNIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd14107   81 SSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQFSKY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGK--YRIP--FYMSTDCENLLKKFLI 286
Cdd:cd14107  161 GSPEFVAPEIVHQEPVSAA-TDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVvsWDTPeiTHLSEDAKDFIKRVLQ 239
                        250
                 ....*....|....*..
gi 564332436 287 LNPSKRGTLEQIMKDRW 303
Cdd:cd14107  240 PDPEKRPSASECLSHEW 256
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
53-299 1.84e-34

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: 132.72  E-value: 1.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHiLTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNH-PNIVKLF--EVIETEKTLYLVM 129
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYdyEVTDEDDYLYMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYasgGEV-FDYLVAHGR---MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLdADMNIKIADFGFSN---EFTF 202
Cdd:cd14131   82 EC---GEIdLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAKaiqNDTT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKKYDGPEV---------DVWSLGVILYTLVSGSLPFdgQNLKELRERVLR---GKYRIP 270
Cdd:cd14131  158 SIVRDSQVGTLNYMSPEAIKDTSASGEGKpkskigrpsDVWSLGCILYQMVYGKTPF--QHITNPIAKLQAiidPNHEIE 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564332436 271 FymsTDCEN-----LLKKFLILNPSKRGTLEQIM 299
Cdd:cd14131  236 F---PDIPNpdlidVMKRCLQRDPKKRPSIPELL 266
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
59-304 1.90e-34

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: 132.73  E-value: 1.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIdKTQlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKII-KAR-SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLL-LDADMN-IKIADFGFSNEFTFGNKLDTFCGSPPY 215
Cdd:cd14193   90 DRIIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLRVNFGTPEF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PFY-MSTDCENLLKKFLILNPSK 291
Cdd:cd14193  170 LAPEVVNYEFVSFP-TDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFedeEFAdISEEAKDFISKLLIKEKSW 248
                        250
                 ....*....|...
gi 564332436 292 RGTLEQIMKDRWM 304
Cdd:cd14193  249 RMSASEALKHPWL 261
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
52-300 2.37e-34

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: 132.46  E-value: 2.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIID---KTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIE--TEKTLY 126
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF---- 202
Cdd:cd06653   83 IFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTicms 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLR-GKYRIPFYMSTDCENL 280
Cdd:cd06653  163 GTGIKSVTGTPYWMSPEVISGEGY-GRKADVWSVACTVVEMLTEKPPWaEYEAMAAIFKIATQpTKPQLPDGVSDACRDF 241
                        250       260
                 ....*....|....*....|
gi 564332436 281 LKKfLILNPSKRGTLEQIMK 300
Cdd:cd06653  242 LRQ-IFVEEKRRPTAEFLLR 260
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
52-292 2.41e-34

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: 133.01  E-value: 2.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSSL---QKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd07860    1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALK---KIRLDTETEgvpSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGG--EVFDYLVAHGrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-----T 201
Cdd:cd07860   78 FEFLHQDlkKFMDASALTG-IPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFgvpvrT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-----QNLKELR------ERVLRGKYRIP 270
Cdd:cd07860  157 YTHEVVTLW----YRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGdseidQLFRIFRtlgtpdEVVWPGVTSMP 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 564332436 271 FYMST------------------DCENLLKKFLILNPSKR 292
Cdd:cd07860  233 DYKPSfpkwarqdfskvvppldeDGRDLLSQMLHYDPNKR 272
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
52-285 2.51e-34

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: 135.51  E-value: 2.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR-IMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05621   53 DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFCAFQDDKYLYMVME 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG--FSNEFTFGNKLDT 208
Cdd:cd05621  133 YMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGtcMKMDETGMVHCDT 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQ---GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLL 281
Cdd:cd05621  212 AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFpddvEISKHAKNLI 291

                 ....
gi 564332436 282 KKFL 285
Cdd:cd05621  292 CAFL 295
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
49-303 2.69e-34

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: 133.59  E-value: 2.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  49 HIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdkTQLNSSSLQKL--FREVRIMKVLNHPNIVKLFEVI------- 119
Cdd:cd07866    6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKI--LMHNEKDGFPItaLREIKILKKLKHPNVVPLIDMAverpdks 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 120 -ETEKTLYLVMEYA----SGgevfdyLVAHGRMKEKEARAK--FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIA 192
Cdd:cd07866   84 kRKRGSVYMVTPYMdhdlSG------LLENPSVKLTESQIKcyMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 193 DFGFSNEFTfGNKLDTFCGSPP-------------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSG------------- 246
Cdd:cd07866  158 DFGLARPYD-GPPPNPKGGGGGgtrkytnlvvtrwYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRrpilqgksdidql 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 247 -------------------SLP-FDGQNLKELRERVLRGKYRipfYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07866  237 hlifklcgtpteetwpgwrSLPgCEGVHSFTNYPRTLEERFG---KLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
53-325 3.10e-34

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: 133.80  E-value: 3.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI-----ETEKTLYL 127
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILrppspEEFNDVYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYAsggEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNeftfgnk 205
Cdd:cd07834   82 VTELM---ETDLHKVIKSPQPLTDDHIQYflYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLAR------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 ldTFCGSPP------------YAAPEL-FQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQN------------------ 254
Cdd:cd07834  152 --GVDPDEDkgflteyvvtrwYRAPELlLSSKKYTKA-IDIWSVGCIFAELLTRKPLFPGRDyidqlnlivevlgtpsee 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 255 -------------LKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGH-EDDElkPYVEPL 320
Cdd:cd07834  229 dlkfissekarnyLKSLPKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHdPEDE--PVAKPP 306

                 ....*
gi 564332436 321 PDYKD 325
Cdd:cd07834  307 FDFPF 311
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
52-299 3.33e-34

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: 132.07  E-value: 3.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSSLQKLF-REVRIMKVL-NHPNIVKLF--EVI--ETEKTL 125
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEQLRVAiKEIEIMKRLcGHPNIVQYYdsAILssEGRKEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYAsGGEVFDYL--VAHGRMKEKEARAKFRQIVSAVQYCHQKF--IVHRDLKAENLLLDADMNIKIADFG-FSNEF 200
Cdd:cd13985   78 LLLMEYC-PGSLVDILekSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsATTEH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TFGNKLDTfCG----------SPPYAAPELFQ--GKKYDGPEVDVWSLGVILYTLVSGSLPFDGqnlkELRERVLRGKYR 268
Cdd:cd13985  157 YPLERAEE-VNiieeeiqkntTPMYRAPEMIDlySKKPIGEKADIWALGCLLYKLCFFKLPFDE----SSKLAIVAGKYS 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 269 IPF--YMSTDCENLLKKFLILNPSKRGTLEQIM 299
Cdd:cd13985  232 IPEqpRYSPELHDLIRHMLTPDPAERPDIFQVI 264
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
59-300 3.98e-34

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: 131.41  E-value: 3.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTC-RETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-----FTFGNKLdtfcGS 212
Cdd:cd05041   82 TFLRKKGaRLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedgeYTVSDGL----KQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PP--YAAPELFQGKKYDGpEVDVWSLGVILY-TLVSGSLPFDGQNLKELRERVLRGkYRIPF--YMSTDCENLLKKFLIL 287
Cdd:cd05041  158 IPikWTAPEALNYGRYTS-ESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIESG-YRMPApeLCPEAVYRLMLQCWAY 235
                        250
                 ....*....|...
gi 564332436 288 NPSKRGTLEQIMK 300
Cdd:cd05041  236 DPENRPSFSEIYN 248
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-250 5.64e-34

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: 132.19  E-value: 5.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKiidKT-QLNSSSLQKLFR---EVRIMKVLNHPNIVKLFEV------IETEKTLYLV 128
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIK---KCrQELSPSDKNRERwclEVQIMKKLNHPNVVSARDVppelekLSPNDLPLLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYL----VAHGrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFT 201
Cdd:cd13989   78 MEYCSGGDLRKVLnqpeNCCG-LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqqgGGRVIYKLIDLGYAKELD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564332436 202 FGNKLDTFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd13989  157 QGSLCTSFVGTLQYLAPELFESKKYTC-TVDYWSFGTLAFECITGYRPF 204
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
53-317 9.69e-34

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: 131.77  E-value: 9.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTFCG 211
Cdd:cd06655   99 AGGSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITpEQSKRSTMVG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENLL 281
Cdd:cd06655  178 TPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSPIFRDFL 249
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYV 317
Cdd:cd06655  250 NRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLI 285
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
53-317 1.10e-33

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: 131.38  E-value: 1.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTFCG 211
Cdd:cd06656   99 AGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMVG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENLL 281
Cdd:cd06656  178 TPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPERLSAVFRDFL 249
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYV 317
Cdd:cd06656  250 NRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLI 285
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
52-250 1.13e-33

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: 130.55  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSSLQK------LFREVRIMKVLNHPNIVKLFEVIE--TEK 123
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVK---QVQFDPESPETskevnaLECEIQLLKNLLHERIVQYYGCLRdpQER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF- 202
Cdd:cd06652   80 TLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTi 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 203 ---GNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd06652  160 clsGTGMKSVTGTPYWMSPEVISGEGY-GRKADIWSVGCTVVEMLTEKPPW 209
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
52-303 1.34e-33

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: 131.19  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNS-------SSLqklfREVRIMKVLNHPNIVKLFEVI--ETE 122
Cdd:cd07843    6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALK---KLKMEKekegfpiTSL----REINILLKLQHPNIVTVKEVVvgSNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVMEYasggevfdylVAHG------RMKEK----EARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIA 192
Cdd:cd07843   79 DKIYMVMEY----------VEHDlkslmeTMKQPflqsEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKIC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 193 DFGFSNEFtfgnkldtfcGSPP-----------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN------- 254
Cdd:cd07843  149 DFGLAREY----------GSPLkpytqlvvtlwYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSeidqlnk 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 255 -LKEL---RERV----------------------LRGKYRIPFyMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07843  219 iFKLLgtpTEKIwpgfselpgakkktftkypynqLRKKFPALS-LSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
53-301 2.73e-33

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: 130.32  E-value: 2.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVK--IIDKTQLNssslqklfREVRIMKVLNHPNIVKL---FEVIETEKT--- 124
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDKRYKN--------RELQIMRRLKHPNIVKLkyfFYSSGEKKDevy 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEY--------ASggevfDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFG 195
Cdd:cd14137   78 LNLVMEYmpetlyrvIR-----HYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 FSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN-LKELRE--RVL--------- 263
Cdd:cd14137  153 SAKRLVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESsVDQLVEiiKVLgtptreqik 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 264 ---RGKYRIPF--------------YMSTDCENLLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd14137  233 amnPNYTEFKFpqikphpwekvfpkRTPPDAIDLLSKILVYNPSKRLTALEALAH 287
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
53-324 3.40e-33

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: 131.14  E-value: 3.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVK-IIDKTQlNSSSLQKLFREVRIMKVLN-HPNIVKLFEVI--ETEKTLYLV 128
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAFR-NATDAQRTFREIMFLQELNdHPNIIKLLNVIraENDKDIYLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 meyasggevFDYL-------VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT 201
Cdd:cd07852   88 ---------FEYMetdlhavIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNKldtfCGSPP----------YAAPE-LFQGKKYD-GpeVDVWSLGVILYTLVSGSLPFDGQN-LKELrERVLR--GK 266
Cdd:cd07852  159 QLEE----DDENPvltdyvatrwYRAPEiLLGSTRYTkG--VDMWSVGCILGEMLLGKPLFPGTStLNQL-EKIIEviGR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 267 ----------------------YRIPFYM-------STDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGH-EDDEL--- 313
Cdd:cd07852  232 psaediesiqspfaatmleslpPSRPKSLdelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHnPADEPslp 311
                        330
                 ....*....|.
gi 564332436 314 KPYVEPLPDYK 324
Cdd:cd07852  312 GPIVIPLDDNK 322
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
56-292 4.77e-33

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: 129.23  E-value: 4.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNS-SSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05608    6 FRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKrKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEV--FDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTF 209
Cdd:cd05608   86 GDLryHIYNVDEENPGFQEPRACFytAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGqTKTKGY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF--DGQNL--KELRERVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd05608  166 AGTPGFMAPELLLGEEYD-YSVDYFTLGVTLYEMIAARGPFraRGEKVenKELKQRILNDSVTYSEKFSPASKSICEALL 244

                 ....*..
gi 564332436 286 ILNPSKR 292
Cdd:cd05608  245 AKDPEKR 251
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
53-314 5.51e-33

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: 128.99  E-value: 5.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06643    7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK--SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFC 210
Cdd:cd06643   85 AGGAVDAVMLELERpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTlQRRDSFI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELF-----QGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGK---YRIPFYMSTDCENLLK 282
Cdd:cd06643  165 GTPYWMAPEVVmcetsKDRPYDY-KADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFLR 243
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564332436 283 KFLILNPSKRGTLEQIMKDRWMNVGHEDDELK 314
Cdd:cd06643  244 KCLEKNVDARWTTSQLLQHPFVSVLVSNKPLR 275
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
97-304 5.68e-33

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: 128.01  E-value: 5.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  97 LFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVMEYASGGEVF--DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVH 173
Cdd:cd14109   43 LMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 174 RDLKAENLLLDADmNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQ 253
Cdd:cd14109  123 LDLRPEDILLQDD-KLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPV-TLATDMWSVGVLTYVLLGGISPFLGD 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 254 NLKELRERVLRGKYR----IPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14109  201 NDRETLTNVRSGKWSfdssPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
59-303 7.24e-33

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: 127.77  E-value: 7.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSsslQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM---NIKIADFGFSNEFTFGNKLDTFCGSPPY 215
Cdd:cd14115   78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHRHVHHLLGNPEF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 216 AAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFL--IL--NPSK 291
Cdd:cd14115  158 AAPEVIQGTPVS-LATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFInvILqeDPRR 236
                        250
                 ....*....|..
gi 564332436 292 RGTLEQIMKDRW 303
Cdd:cd14115  237 RPTAATCLQHPW 248
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
53-304 7.36e-33

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: 128.02  E-value: 7.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT--FGNKLDTFC 210
Cdd:cd14111   82 SGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNplSLRQLGRRT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRiPFYM----STDCENLLKKFLI 286
Cdd:cd14111  162 GTLEYMAPEMVKGEPV-GPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLypnvSQSASLFLKKVLS 239
                        250
                 ....*....|....*...
gi 564332436 287 LNPSKRGTLEQIMKDRWM 304
Cdd:cd14111  240 SYPWSRPTTKDCFAHAWL 257
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
53-300 7.91e-33

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: 129.00  E-value: 7.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETK--SEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS--NEFTFgNKLDTF 209
Cdd:cd06644   92 PGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSakNVKTL-QRRDSF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKY-DGP---EVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGK---YRIPFYMSTDCENLLK 282
Cdd:cd06644  171 IGTPYWMAPEVVMCETMkDTPydyKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLK 250
                        250
                 ....*....|....*...
gi 564332436 283 KFLILNPSKRGTLEQIMK 300
Cdd:cd06644  251 TALDKHPETRPSAAQLLE 268
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
52-303 9.22e-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: 128.37  E-value: 9.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKII--DKTQLNSSSLqklFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd07836    1 NFKQLEKLGEGTYATVYKGRNRTTGEIVALKEIhlDAEEGTPSTA---IREISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGgEVFDYLVAHGR---MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-----T 201
Cdd:cd07836   78 EYMDK-DLKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFgipvnT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR----------------G 265
Cdd:cd07836  157 FSNEVVTLW----YRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRimgtptestwpgisqlP 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 266 KYR--IPFYMSTDCEN-----------LLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07836  233 EYKptFPRYPPQDLQQlfphadplgidLLHRLLQLNPELRISAHDALQHPW 283
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
52-329 1.14e-32

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: 129.39  E-value: 1.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRimKVLNHPN---IVKLFEVIETEKTLYLV 128
Cdd:cd05597    2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREER--DVLVNGDrrwITKLHYAFQDENYLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLD 207
Cdd:cd05597   80 MDYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 --TFCGSPPYAAPELFQ----GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVL--RGKYRIPFY---MSTD 276
Cdd:cd05597  160 ssVAVGTPDYISPEILQamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPDDeddVSEE 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 277 CENLLKKfLILNPSKR---GTLEQIMKDRWMNvGHEDDELK----PYVeplPDYKDPRRT 329
Cdd:cd05597  240 AKDLIRR-LICSRERRlgqNGIDDFKKHPFFE-GIDWDNIRdstpPYI---PEVTSPTDT 294
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
53-299 1.15e-32

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: 128.18  E-value: 1.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdkTQLNSSSLQKLFREVRIMKVLNHPNIVKL--FEVIETE---KTLYL 127
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKI--LCHSKEDVKEAMREIENYRLFNHPNILRLldSQIVKEAggkKEVYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYL----VAHGRMKEKEARAKFRQIVSAVQYCHQKFIV---HRDLKAENLLLDADMNIKIADFGFSNE- 199
Cdd:cd13986   80 LLPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSMNPa 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 --FTFGNKL-------DTFCGSPPYAAPELFQGKKY---DgPEVDVWSLGVILYTLVSGSLPFD--GQNLKELRERVLRG 265
Cdd:cd13986  160 riEIEGRREalalqdwAAEHCTMPYRAPELFDVKSHctiD-EKTDIWSLGCTLYALMYGESPFEriFQKGDSLALAVLSG 238
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564332436 266 KYRIP--FYMSTDCENLLKKFLILNPSKRGTLEQIM 299
Cdd:cd13986  239 NYSFPdnSRYSEELHQLVKSMLVVNPAERPSIDDLL 274
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
59-299 1.36e-32

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: 128.18  E-value: 1.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFCGSPPYAA 217
Cdd:cd06659  107 D-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDvPKRKSLVGTPYWMA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 218 PELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDG----QNLKELRER---VLRGKYRIpfymSTDCENLLKKFLILNPS 290
Cdd:cd06659  186 PEVISRCPY-GTEVDIWSLGIMVIEMVDGEPPYFSdspvQAMKRLRDSpppKLKNSHKA----SPVLRDFLERMLVRDPQ 260

                 ....*....
gi 564332436 291 KRGTLEQIM 299
Cdd:cd06659  261 ERATAQELL 269
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
56-292 1.43e-32

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 129.36  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKT---QLNSSSLQKLFREvrIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd05598    6 IKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKdvlKRNQVAHVKAERD--ILAEADNEWVVKLYYSFQDKENLYFVMDYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFC-- 210
Cdd:cd05598   84 PGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYLah 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 ---GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVL--RGKYRIPFY--MSTDCENLLKK 283
Cdd:cd05598  164 slvGTPNYIAPEVLLRTGY-TQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLSPEAKDLILR 242

                 ....*....
gi 564332436 284 fLILNPSKR 292
Cdd:cd05598  243 -LCCDAEDR 250
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
59-301 2.74e-32

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: 126.37  E-value: 2.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIPER--DSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAH-GRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDA-DMNIKIADFGFSNEFTFGNKL-DTFCGSP 213
Cdd:cd06624   94 ALLRSKwGPLKDNENTIGYytKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCtETFTGTL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELF-QGKKYDGPEVDVWSLGVILYTLVSGSLPFdgqnlKELRE------RVlrGKYR----IPFYMSTDCENLLK 282
Cdd:cd06624  174 QYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPF-----IELGEpqaamfKV--GMFKihpeIPESLSEEAKSFIL 246
                        250
                 ....*....|....*....
gi 564332436 283 KFLILNPSKRGTLEQIMKD 301
Cdd:cd06624  247 RCFEPDPDKRATASDLLQD 265
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
52-292 3.00e-32

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: 126.46  E-value: 3.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKV-KLARHILTGKEVAVKIIDKTQLN--------SSSLQKLFREVRIMK-VLNHPNIVKLFEVIET 121
Cdd:cd08528    1 EYAVLELLGSGAFGCVyKVRKKSNGQTLLALKEINMTNPAfgrteqerDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 122 EKTLYLVMEYASG---GEVFDYLV-AHGRMKEKEARAKFRQIVSAVQYCH-QKFIVHRDLKAENLLLDADMNIKIADFGF 196
Cdd:cd08528   81 NDRLYIVMELIEGaplGEHFSSLKeKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 197 SNEFTF-GNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYM- 273
Cdd:cd08528  161 AKQKGPeSSKMTSVVGTILYSCPEIVQNEPY-GEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEGMy 239
                        250
                 ....*....|....*....
gi 564332436 274 STDCENLLKKFLILNPSKR 292
Cdd:cd08528  240 SDDITFVIRSCLTPDPEAR 258
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
48-322 3.14e-32

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: 128.46  E-value: 3.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  48 PHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLY 126
Cdd:cd05610    1 PSIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMiNKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS--------- 197
Cdd:cd05610   81 LVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnreln 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 ----------------NEFTFGNKL-----------------------------DTFCGSPPYAAPELFQGKKYdGPEVD 232
Cdd:cd05610  161 mmdilttpsmakpkndYSRTPGQVLslisslgfntptpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPH-GPAVD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 233 VWSLGVILYTLVSGSLPFDGQNLKELRERVLrgKYRIPF-----YMSTDCENLLKKFLILNPSKRGTLEQIMKDR----- 302
Cdd:cd05610  240 WWALGVCLFEFLTGIPPFNDETPQQVFQNIL--NRDIPWpegeeELSVNAQNAIEILLTMDPTKRAGLKELKQHPlfhgv 317
                        330       340
                 ....*....|....*....|.
gi 564332436 303 -WMNVGHEDdelKPYVePLPD 322
Cdd:cd05610  318 dWENLQNQT---MPFI-PQPD 334
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
47-329 4.20e-32

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: 129.74  E-value: 4.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  47 QPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRimKVLNHPN---IVKLFEVIETEK 123
Cdd:cd05624   68 QLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREER--NVLVNGDcqwITTLHYAFQDEN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVA-HGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSN 198
Cdd:cd05624  146 YLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGsclkMND 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFTFGNKLDTfcGSPPYAAPELFQGK-----KYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY- 272
Cdd:cd05624  226 DGTVQSSVAV--GTPDYISPEILQAMedgmgKY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPs 302
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 273 ----MSTDCENLLKKFLILNPSKRGT--LEQIMKD------RWMNVGHEDdelKPYVeplPDYKDPRRT 329
Cdd:cd05624  303 hvtdVSEEAKDLIQRLICSRERRLGQngIEDFKKHaffeglNWENIRNLE---APYI---PDVSSPSDT 365
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
53-300 6.97e-32

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: 125.95  E-value: 6.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESE-DDPVIKKIaLREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGgEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTF 209
Cdd:cd07847   82 CDH-TVLNELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTgPGDDYTDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGS----------------------LP-----------FDGQNLK 256
Cdd:cd07847  161 VATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQplwpgksdvdqlylirktlgdlIPrhqqifstnqfFKGLSIP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564332436 257 ELRERV-LRGKYRipfYMSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd07847  241 EPETREpLESKFP---NISSPALSFLKGCLQMDPTERLSCEELLE 282
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
54-298 7.93e-32

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: 124.71  E-value: 7.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHilTGKEVAVKIIDktqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVMEYA 132
Cdd:cd05082    9 KLLQTIGKGEFGDVMLGDY--RGNKVAVKCIK----NDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKgGLYIVTEYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGR-MKEKEARAKFRQIVS-AVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKLDTFC 210
Cdd:cd05082   83 AKGSLVDYLRSRGRsVLGGDCLLKFSLDVCeAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEAS--STQDTGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG-KYRIPFYMSTDCENLLKKFLILN 288
Cdd:cd05082  161 LPVKWTAPEALREKKFS-TKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKGyKMDAPDGCPPAVYDVMKNCWHLD 239
                        250
                 ....*....|
gi 564332436 289 PSKRGTLEQI 298
Cdd:cd05082  240 AAMRPSFLQL 249
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
59-304 1.54e-31

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: 124.18  E-value: 1.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS-------LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENkdrkksmLDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLDT--- 208
Cdd:cd06628   88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLE-ANSLSTknn 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 -----FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFdgQNLKELRERVLRGKY---RIPFYMSTDCENL 280
Cdd:cd06628  167 garpsLQGSVFWMAPEVVKQTSYT-RKADIWSLGCLVVEMLTGTHPF--PDCTQMQAIFKIGENaspTIPSNISSEARDF 243
                        250       260
                 ....*....|....*....|....
gi 564332436 281 LKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd06628  244 LEKTFEIDHNKRPTADELLKHPFL 267
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
75-305 1.55e-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: 125.53  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  75 TGKEVAVKIIdktqlnsSSLQKLFREVRI-MKVLNHPNIVKLFEVIE----TEKTLYLVMEYASGGEVFDYLVAHG--RM 147
Cdd:cd14170   26 TQEKFALKML-------QDCPKARREVELhWRASQCPHIVRIVDVYEnlyaGRKCLLIVMECLDGGELFSRIQDRGdqAF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 148 KEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA---DMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGK 224
Cdd:cd14170   99 TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 225 KYDgPEVDVWSLGVILYTLVSGSLPFDGQN----LKELRERVLRGKYRIP----FYMSTDCENLLKKFLILNPSKRGTLE 296
Cdd:cd14170  179 KYD-KSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPnpewSEVSEEVKMLIRNLLKTEPTQRMTIT 257

                 ....*....
gi 564332436 297 QIMKDRWMN 305
Cdd:cd14170  258 EFMNHPWIM 266
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-250 1.63e-31

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: 125.03  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL-----YLVMEYAS 133
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSC-RLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGR---MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL-DADMNI--KIADFGFSNEFTFGNKLD 207
Cdd:cd14039   80 GGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDLDQGSLCT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564332436 208 TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd14039  160 SFVGTLQYLAPELFENKSYT-VTVDYWSFGTMVFECIAGFRPF 201
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
49-285 1.78e-31

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: 127.82  E-value: 1.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  49 HIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPN-IVKLFEVIETEKTLYL 127
Cdd:cd05623   70 HKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQwITTLHYAFQDDNNLYL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVA-HGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL 206
Cdd:cd05623  150 VMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTV 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DT--FCGSPPYAAPELFQ----GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY-----MST 275
Cdd:cd05623  230 QSsvAVGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPtqvtdVSE 309
                        250
                 ....*....|
gi 564332436 276 DCENLLKKFL 285
Cdd:cd05623  310 NAKDLIRRLI 319
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
53-292 2.79e-31

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: 124.31  E-value: 2.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSL-QKLFREVRIMKVL---NHPNIVKLFEV-----IETEK 123
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV-RVPLSEEGIpLSTIREIALLKQLesfEHPNVVRLLDVchgprTDREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASG--GEVFDYLVAHGrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT 201
Cdd:cd07838   80 KLTLVFEHVDQdlATYLDKCPKPG-LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPF----DGQNLKELRE--------------RVL 263
Cdd:cd07838  159 FEMALTSVVVTLWYRAPEVLLQSSYATP-VDMWSVGCIFAELFNRRPLFrgssEADQLGKIFDviglpseeewprnsALP 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 264 RGKY----RIPF-----YMSTDCENLLKKFLILNPSKR 292
Cdd:cd07838  238 RSSFpsytPRPFksfvpEIDEEGLDLLKKMLTFNPHKR 275
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
50-292 3.32e-31

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: 124.40  E-value: 3.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKII----DKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVIETEKT- 124
Cdd:cd07865   11 VSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmenEKEGFPITAL----REIKILQLLKHENVVNLIEICRTKATp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 -------LYLVMEYAsggevfDYLVA------HGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKI 191
Cdd:cd07865   87 ynrykgsIYLVFEFC------EHDLAgllsnkNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 192 ADFGFSNEFT---------FGNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVIL------------------YTLV 244
Cdd:cd07865  161 ADFGLARAFSlaknsqpnrYTNRVVTLW----YRPPELLLGERDYGPPIDMWGAGCIMaemwtrspimqgnteqhqLTLI 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 245 S---GSL-----P-------FDGQNLKELRERVLRGKYRiPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd07865  237 SqlcGSItpevwPgvdklelFKKMELPQGQKRKVKERLK-PYVKDPYALDLIDKLLVLDPAKR 298
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
56-300 5.25e-31

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: 123.25  E-value: 5.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSS--LQKLFREVRIMKVLNHPNIVKLFEV-IETEKtLYLVMEYA 132
Cdd:cd14046   11 LQVLGKGAFGQVVKVRNKLDGRYYAIK---KIKLRSESknNSRILREVMLLSRLNHQHVVRYYQAwIERAN-LYIQMEYC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDyLVAHGRMKEK-EARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGF--SNEFTF------G 203
Cdd:cd14046   87 EKSTLRD-LIDSGLFQDTdRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLatSNKLNVelatqdI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NKLDTFCGSPP-----------YAAPELFQGKK--YDgPEVDVWSLGVILYTLvsgSLPFDG-----QNLKELRER--VL 263
Cdd:cd14046  166 NKSTSAALGSSgdltgnvgtalYVAPEVQSGTKstYN-EKVDMYSLGIIFFEM---CYPFSTgmervQILTALRSVsiEF 241
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564332436 264 RGKYRIPFYMSTdcENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14046  242 PPDFDDNKHSKQ--AKLIRWLLNHDPAKRPSAQELLK 276
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
53-304 9.50e-31

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: 121.56  E-value: 9.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSsslQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14110    5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDK---QLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL--DTFC 210
Cdd:cd14110   82 SGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLmtDKKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP-FY--MSTDCENLLKKFLIL 287
Cdd:cd14110  162 DYVETMAPELLEGQGA-GPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSrCYagLSGGAVNFLKSTLCA 240
                        250
                 ....*....|....*..
gi 564332436 288 NPSKRGTLEQIMKDRWM 304
Cdd:cd14110  241 KPWGRPTASECLQNPWL 257
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
53-304 1.47e-30

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: 121.26  E-value: 1.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKtqLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL--DADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14191   82 SGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAGSLKVL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PF-YMSTDCENLLKKFL 285
Cdd:cd14191  162 FGTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFddeAFdEISDDAKDFISNLL 240
                        250
                 ....*....|....*....
gi 564332436 286 ILNPSKRGTLEQIMKDRWM 304
Cdd:cd14191  241 KKDMKARLTCTQCLQHPWL 259
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
54-245 1.97e-30

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: 121.72  E-value: 1.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHIL----TGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIET--EKTLYL 127
Cdd:cd05038    7 KFIKQLGEGHFGSVELCRYDPlgdnTGEQVAVKSL-QPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESpgRRSLRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHgrmKEKEARAKF----RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS------ 197
Cdd:cd05038   86 IMEYLPSGSLRDYLQRH---RDQIDLKRLllfaSQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAkvlped 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564332436 198 NEFTFGNKLDTfcgSPPY-AAPELFQGKKYDGpEVDVWSLGVILYTLVS 245
Cdd:cd05038  163 KEYYYVKEPGE---SPIFwYAPECLRESRFSS-ASDVWSFGVTLYELFT 207
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
53-300 2.61e-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: 2.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLN-HPNIVKLFEVIETEKT--LYLVM 129
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLFDRKTgrLALVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGgEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADmNIKIADFGfsneftfgnKLDT 208
Cdd:cd07831   80 ELMDM-NLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG---------SCRG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYA---------APELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN------------------LKELRER 261
Cdd:cd07831  149 IYSKPPYTeyistrwyrAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNeldqiakihdvlgtpdaeVLKKFRK 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564332436 262 VLRGKYRIPF-----------YMSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd07831  229 SRHMNYNFPSkkgtglrkllpNASAEGLDLLKKLLAYDPDERITAKQALR 278
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
57-306 2.78e-30

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 122.56  E-value: 2.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVA---VKIIDKTQLNSSSLQK---------LFREVRIMKVLNHPNIVKLFEVIETEKT 124
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLvgmcgihftTLRELKIMNEIKHENIMGLVDVYVEGDF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASG--GEVFDYLVahgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:PTZ00024  95 INLVMDIMASdlKKVVDRKI---RLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFCGSPP---------------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNlkELRE--RV--L 263
Cdd:PTZ00024 172 PPYSDTLSKDETmqrreemtskvvtlwYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGEN--EIDQlgRIfeL 249
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 264 RGK---------YRIPFYM-----------------STDCENLLKKFLILNPSKRGTLEQIMKDRWMNV 306
Cdd:PTZ00024 250 LGTpnednwpqaKKLPLYTeftprkpkdlktifpnaSDDAIDLLQSLLKLNPLERISAKEALKHEYFKS 318
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
59-307 3.05e-30

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: 121.30  E-value: 3.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRREL--LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFCGSPPYAA 217
Cdd:cd06658  108 D-IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEvPKRKSLVGTPYWMA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 218 PELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDG----QNLKELRERvLRGKYRIPFYMSTDCENLLKKFLILNPSKRG 293
Cdd:cd06658  187 PEVISRLPY-GTEVDIWSLGIMVIEMIDGEPPYFNepplQAMRRIRDN-LPPRVKDSHKVSSVLRGFLDLMLVREPSQRA 264
                        250
                 ....*....|....
gi 564332436 294 TLEQIMKDRWMNVG 307
Cdd:cd06658  265 TAQELLQHPFLKLA 278
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
51-304 3.09e-30

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: 120.87  E-value: 3.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlfrEVRIMKVL-NHPNIVKLFEV------IETEK 123
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKL---EINILRKFsNHPNIATFYGAfikkdpPGGDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDY---LVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE 199
Cdd:cd06608   83 QLWLVMEYCGGGSVTDLvkgLRKKGKRLKEEWIAYIlRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFGN-KLDTFCGSPPYAAPELFQGKKYDGPEV----DVWSLGVILYTLVSGSLPF-DGQNLKELReRVLRG---KYRIP 270
Cdd:cd06608  163 LDSTLgRRNTFIGTPYWMAPEVIACDQQPDASYdarcDVWSLGITAIELADGKPPLcDMHPMRALF-KIPRNpppTLKSP 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564332436 271 FYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd06608  242 EKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-304 3.59e-30

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: 121.50  E-value: 3.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  49 HIgNYR--LLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlnSSSLQKLFrEVRIMKVLNH------PNIVKLFEV-- 118
Cdd:cd14210   10 HI-AYRyeVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKK--RFHQQALV-EVKILKHLNDndpddkHNIVRYKDSfi 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 119 ------IETE---KTLYLVMEyASGGEVFDYLVAHgrmkekearaKF-RQIVSAVQYCHQKFIVHRDLKAENLLL--DAD 186
Cdd:cd14210   86 frghlcIVFEllsINLYELLK-SNNFQGLSLSLIR----------KFaKQILQALQFLHKLNIIHCDLKPENILLkqPSK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 187 MNIKIADFG---FSNEFTFgnkldTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKE------ 257
Cdd:cd14210  155 SSIKVIDFGsscFEGEKVY-----TYIQSRFYRAPEVILGLPYD-TAIDMWSLGCILAELYTGYPLFPGENEEEqlacim 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 258 --------------------------LRERVL-RGKYRIP----FYMSTDCEN-----LLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd14210  229 evlgvppkslidkasrrkkffdsngkPRPTTNsKGKKRRPgsksLAQVLKCDDpsfldFLKKCLRWDPSERMTPEEALQH 308

                 ...
gi 564332436 302 RWM 304
Cdd:cd14210  309 PWI 311
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
59-268 3.73e-30

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: 120.46  E-value: 3.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARhILTGKEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKL--FEVIETEKTLylVMEYASGGE 136
Cdd:cd14066    1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMNCAASK-KEFLTELEMLGRLRHPNLVRLlgYCLESDEKLL--VYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLvaHGRMKEK----EARAKF-RQIVSAVQYCHQKF---IVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN---K 205
Cdd:cd14066   77 LEDRL--HCHKGSPplpwPQRLKIaKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSEsvsK 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFD-------GQNLKELRERVLRGKYR 268
Cdd:cd14066  155 TSAVKGTIGYLAPEYIRTGRVS-TKSDVYSFGVVLLELLTGKPAVDenrenasRKDLVEWVESKGKEELE 223
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
54-304 4.63e-30

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: 119.64  E-value: 4.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKT---IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETE--KTLYLV 128
Cdd:cd13983    1 RYLKFnevLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKskKEVIFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCH--QKFIVHRDLKAENLLLDADMN-IKIADFGFSNEfTFGNK 205
Cdd:cd13983   81 TELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHtrDPPIIHRDLKCDNIFINGNTGeVKIGDLGLATL-LRQSF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPELFQGkKYDgPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRGKYRIPFYMSTDCEnlLKKF 284
Cdd:cd13983  160 AKSVIGTPEFMAPEMYEE-HYD-EKVDIYAFGMCLLEMATGEYPYsECTNAAQIYKKVTSGIKPESLSKVKDPE--LKDF 235
                        250       260
                 ....*....|....*....|...
gi 564332436 285 L---ILNPSKRGTLEQIMKDRWM 304
Cdd:cd13983  236 IekcLKPPDERPSARELLEHPFF 258
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
52-300 5.83e-30

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: 120.22  E-value: 5.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGG--EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-----TFGN 204
Cdd:cd07861   81 LSMDlkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFgipvrVYTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCgsppYAAPELFQG-KKYDGPeVDVWSLGVILYTLVSGSLPFDGQN-----------LKELRERVLRGKYRIPFY 272
Cdd:cd07861  161 EVVTLW----YRAPEVLLGsPRYSTP-VDIWSIGTIFAEMATKKPLFHGDSeidqlfrifriLGTPTEDIWPGVTSLPDY 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 273 MST------------------DCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd07861  236 KNTfpkwkkgslrtavknldeDGLDLLEKMLIYDPAKRISAKKALV 281
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
70-304 9.60e-30

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: 118.30  E-value: 9.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  70 ARHILTGKEVAVKIIDKTQLNSSsLQKLFRevrimkVLNHPNIVKLFEVIETEKTLYLVMEYASGgEVFDYLVAHGRMKE 149
Cdd:cd13976   12 CVDIHTGEELVCKVVPVPECHAV-LRAYFR------LPSHPNISGVHEVIAGETKAYVFFERDHG-DLHSYVRSRKRLRE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 150 KEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFC---GSPPYAAPELFQ-GKK 225
Cdd:cd13976   84 PEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGEDDSLSdkhGCPAYVSPEILNsGAT 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 226 YDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd13976  164 YSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
54-314 1.40e-29

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: 119.08  E-value: 1.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVMEYA 132
Cdd:cd06620    8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDA-KSSVRKQILRELQILHECHSPYIVSFYGAFLNENnNIIICMEYM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKE----KEARAkfrqIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKL- 206
Cdd:cd06620   87 DCGSLDKILKKKGPFPEevlgKIAVA----VLEGLTYLYNVHrIIHRDIKPSNILVNSKGQIKLCDFGVSGELI--NSIa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQN-----------LKELRERVL-----RGKYRIP 270
Cdd:cd06620  161 DTFVGTSTYMSPERIQGGKY-SVKSDVWSLGLSIIELALGEFPFAGSNddddgyngpmgILDLLQRIVnepppRLPKDRI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 271 FymSTDCENLLKKFLILNPSKRGTLEQIM-KDRWMNVGHE-DDELK 314
Cdd:cd06620  240 F--PKDLRDFVDRCLLKDPRERPSPQLLLdHDPFIQAVRAsDVDLR 283
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
59-300 1.66e-29

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: 119.36  E-value: 1.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFCGSPPYAA 217
Cdd:cd06657  106 D-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPRRKSLVGTPYWMA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 218 PELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQ----NLKELRERvLRGKYRIPFYMSTDCENLLKKFLILNPSKRG 293
Cdd:cd06657  185 PELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEpplkAMKMIRDN-LPPKLKNLHKVSPSLKGFLDRLLVRDPAQRA 262

                 ....*..
gi 564332436 294 TLEQIMK 300
Cdd:cd06657  263 TAAELLK 269
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
57-252 1.72e-29

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: 118.22  E-value: 1.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTG---KEVAVKIIDKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVIETEkTLYLVMEYAS 133
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMKSgkeVEVAVKTLKQEHEKAGK-KEFLREASVMAQLDHPCIVRLIGVCKGE-PLMLVMELAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF--CG 211
Cdd:cd05060   79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRAttAG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564332436 212 SPP--YAAPELFQGKKYDGPEvDVWSLGVILYTLVS-GSLPFDG 252
Cdd:cd05060  159 RWPlkWYAPECINYGKFSSKS-DVWSYGVTLWEAFSyGAKPYGE 201
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
53-343 2.13e-29

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 123.06  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI--------ETEKT 124
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKCHEDFakkdprnpENVLM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDYLVAHGR----MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF 200
Cdd:PTZ00283 114 IALVLDYANAGDLRQEIKSRAKtnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TFGNKLD---TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTD 276
Cdd:PTZ00283 194 AATVSDDvgrTFCGTPYYVAPEIWRRKPYS-KKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDpLPPSISPE 272
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332436 277 CENLLKKFLILNPSKRGTLEQIMK----DRWMNVgheddeLKPYVEPLPDYKDPRRTELMVSMGYTREEIQ 343
Cdd:PTZ00283 273 MQEIVTALLSSDPKRRPSSSKLLNmpicKLFISG------LLEIVQTQPGFSGPLRDTISRQIQQTKQLLQ 337
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
52-292 2.57e-29

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: 120.72  E-value: 2.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05629    2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMfKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF---------- 200
Cdd:cd05629   82 FLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFhkqhdsayyq 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 -------------------------TFGNK--LDTF-----------CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYT 242
Cdd:cd05629  162 kllqgksnknridnrnsvavdsinlTMSSKdqIATWkknrrlmaystVGTPDYIAPEIFLQQGY-GQECDWWSLGAIMFE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564332436 243 LVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKfLILNPSKR 292
Cdd:cd05629  241 CLIGWPPFCSENSHETYRKIINWRETLYFpddiHLSVEAEDLIRR-LITNAENR 293
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
53-292 3.78e-29

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: 117.82  E-value: 3.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd05630   82 MNGGDLKFHIYHMGQAGFPEARAVFyaAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYD-GPevDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR------GKYRIPFymSTDCENLLK 282
Cdd:cd05630  162 VGTVGYMAPEVVKNERYTfSP--DWWALGCLLYEMIAGQSPFQQRKKKIKREEVERlvkevpEEYSEKF--SPQARSLCS 237
                        250
                 ....*....|
gi 564332436 283 KFLILNPSKR 292
Cdd:cd05630  238 MLLCKDPAER 247
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
52-300 3.79e-29

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: 117.21  E-value: 3.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSslqKLFREVRIMKVLNHPNIVKLF--------------- 116
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIK---RVKLNNE---KAEREVKALAKLDHPNIVRYNgcwdgfdydpetsss 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 117 -EVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEK--EARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIAD 193
Cdd:cd14047   81 nSSRSKTKCLFIQMEFCEKGTLESWIEKRNGEKLDkvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 194 FGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLpfDGQNLKELRERVLRGKYRIPFYM 273
Cdd:cd14047  161 FGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDY-GKEVDIYALGLILFELLHVCD--SAFEKSKFWTDLRNGILPDIFDK 237
                        250       260
                 ....*....|....*....|....*...
gi 564332436 274 STDCEN-LLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14047  238 RYKIEKtIIKKMLSKKPEDRPNASEILR 265
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
52-250 4.14e-29

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: 117.49  E-value: 4.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIID---KTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIE--TEKTLY 126
Cdd:cd06651    8 NWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF---- 202
Cdd:cd06651   88 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicms 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd06651  168 GTGIRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPW 214
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
59-252 4.46e-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: 117.17  E-value: 4.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLvaHGRMKEKEARAKFR---QIVSAVQYCH--QKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF------GNKLD 207
Cdd:cd13978   81 SLL--EREIQDVPWSLRFRiihEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKsisanrRRGTE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGPEV-DVWSLGVILYTLVSGSLPFDG 252
Cdd:cd13978  159 NLGGTPIYMAPEAFDDFNKKPTSKsDVYSFAIVIWAVLTRKEPFEN 204
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
109-303 5.31e-29

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: 116.30  E-value: 5.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 109 HPNIVKLFEVIETEKTLYLVMEyASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN 188
Cdd:cd14023   44 HRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEER 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 189 IKIADFGFSNEFTFGNKLDTFC---GSPPYAAPELFQGK-KYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR 264
Cdd:cd14023  123 TQLRLESLEDTHIMKGEDDALSdkhGCPAYVSPEILNTTgTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRR 202
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564332436 265 GKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14023  203 GQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-250 6.09e-29

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: 117.37  E-value: 6.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------YLVMEYA 132
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQC-RQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGR---MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGNKL 206
Cdd:cd14038   81 QGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqgEQRLIHKIIDLGYAKELDQGSLC 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd14038  161 TSFVGTLQYLAPELLEQQKYT-VTVDYWSFGTLAFECITGFRPF 203
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
59-301 6.13e-29

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: 116.26  E-value: 6.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVklARHILTGK-EVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd05085    4 LGKGNFGEV--YKGTLKDKtPVAVKTC-KEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLvahgrmKEKEARAKFRQIV-------SAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd05085   81 LSFL------RKKKDELKTKQLVkfsldaaAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRI--PFYMSTDCENLLKKFL 285
Cdd:cd05085  155 KQIPikWTAPEALNYGRYSS-ESDVWSFGILLWETFSlGVCPYPGMTNQQAREQVEKG-YRMsaPQRCPEDIYKIMQRCW 232
                        250
                 ....*....|....*.
gi 564332436 286 ILNPSKRGTLEQIMKD 301
Cdd:cd05085  233 DYNPENRPKFSELQKE 248
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
53-304 7.15e-29

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: 117.60  E-value: 7.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIeTEK--------- 123
Cdd:cd07864    9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIV-TDKqdaldfkkd 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 --TLYLVMEYASG---GEVFDYLVahgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN 198
Cdd:cd07864   88 kgAFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLAR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFT------FGNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTL---------------------VSGS---- 247
Cdd:cd07864  165 LYNseesrpYTNKVITLW----YRPPELLLGEERYGPAIDVWSCGCILGELftkkpifqanqelaqlelisrLCGSpcpa 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 248 -------LP-FDGQNLKELRERVLRGKYRipfYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd07864  241 vwpdvikLPyFNTMKPKKQYRRRLREEFS---FIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
52-303 7.60e-29

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: 117.15  E-value: 7.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKII----DKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVIETEKTLYL 127
Cdd:cd07839    1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVrlddDDEGVPSSAL----REICLLKELKHKNIVRLYDVLHSDKKLTL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGG--EVFDYLvaHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF----- 200
Cdd:cd07839   77 VFEYCDQDlkKYFDSC--NGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFgipvr 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TFGNKLDTFCGSPPYAapeLFQGKKYDgPEVDVWSLGVILYTLVSGSLP-FDGQNLKELRERVLR-----------GKYR 268
Cdd:cd07839  155 CYSAEVVTLWYRPPDV---LFGAKLYS-TSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRllgtpteeswpGVSK 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564332436 269 IPFY------------------MSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07839  231 LPDYkpypmypattslvnvvpkLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
59-292 7.81e-29

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: 116.77  E-value: 7.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVL-----NHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstggDCPFIVCMTYAFQTPDKLCFILDLMN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLDTFCGSP 213
Cdd:cd05606   82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFS-KKKPHASVGTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQ-GKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRE---RVLRGKYRIPFYMSTDCENLLKKFLILNP 289
Cdd:cd05606  161 GYMAPEVLQkGVAYDSS-ADWFSLGCMLYKLLKGHSPFRQHKTKDKHEidrMTLTMNVELPDSFSPELKSLLEGLLQRDV 239

                 ...
gi 564332436 290 SKR 292
Cdd:cd05606  240 SKR 242
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
46-250 8.14e-29

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: 117.64  E-value: 8.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  46 EQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnssslQKLFREVRIMKVLN-HPNIVKLFEVI--ETE 122
Cdd:cd14132   13 EWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKK-----KKIKREIKILQNLRgGPNIVKLLDVVkdPQS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVMEYASGgEVFDYLVahGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN-IKIADFGFSnEFT 201
Cdd:cd14132   88 KTPSLIFEYVNN-TDFKTLY--PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA-EFY 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 202 F-GNKLDTFCGSPPYAAPELFQG-KKYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd14132  164 HpGQEYNVRVASRYYKGPELLVDyQYYD-YSLDMWSLGCMLASMIFRKEPF 213
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
51-250 8.26e-29

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: 117.14  E-value: 8.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdkTQLNSSSLQK-LFREVRIMKVLNHPNIVKLFE--VIETEKTLYL 127
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTI--TTDPNPDVQKqILRELEINKSCASPYIVKYYGafLDEQDSSIGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVfDYLvaHGRMKEKEARAKFR-------QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEf 200
Cdd:cd06621   79 AMEYCEGGSL-DSI--YKKVKKKGGRIGEKvlgkiaeSVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGE- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 201 tFGNKLD-TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd06621  155 -LVNSLAgTFTGTSYYMAPERIQGGPYS-ITSDVWSLGLTLLEVAQNRFPF 203
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
55-300 9.49e-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: 116.01  E-value: 9.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARhiLTGK-EVAVKIIDKTQLNSsslQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05059    8 FLKELGSGQFGVVHLGK--WRGKiDVAIKMIKEGSMSE---DDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLvahGRMKEKEARAKF----RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFT--F 202
Cdd:cd05059   83 NGCLLNYL---RERRGKFQTEQLlemcKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLAryvldDEYTssV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTfcgspPYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRI--PFYMSTDCEN 279
Cdd:cd05059  160 GTKFPV-----KWSPPEVFMYSKFSS-KSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQG-YRLyrPHLAPTEVYT 232
                        250       260
                 ....*....|....*....|.
gi 564332436 280 LLKKFLILNPSKRGTLEQIMK 300
Cdd:cd05059  233 IMYSCWHEKPEERPTFKILLS 253
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
51-300 1.14e-28

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: 116.23  E-value: 1.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRL--LKTIGKGNFAKVKLARHILTGKEVAVKII---DKTQLNSsslqkLFREVRIMKVL-NHPNIVKLFE------- 117
Cdd:cd14037    1 GSHHVtiEKYLAEGGFAHVYLVKTSNGGNRAALKRVyvnDEHDLNV-----CKREIEIMKRLsGHKNIVGYIDssanrsg 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 118 --VIEtektLYLVMEYASGGEVFDYLVA--HGRMKEKEARAKFRQIVSAVQYCH--QKFIVHRDLKAENLLLDADMNIKI 191
Cdd:cd14037   76 ngVYE----VLLLMEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 192 ADFG-FSNEFTFGNKLDTFC---------GSPPYAAPE---LFQGKKYDGPeVDVWSLGVILYTLVSGSLPF-DGQNLKe 257
Cdd:cd14037  152 CDFGsATTKILPPQTKQGVTyveedikkyTTLQYRAPEmidLYRGKPITEK-SDIWALGCLLYKLCFYTTPFeESGQLA- 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564332436 258 lrerVLRGKYRIPFY--MSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14037  230 ----ILNGNFTFPDNsrYSKRLHKLIRYMLEEDPEKRPNIYQVSY 270
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
53-254 1.15e-28

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: 116.63  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGG--EVFDYLvAHGRMKEKeARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLD--T 208
Cdd:cd07848   83 EKNmlELLEEM-PNGVPPEK-VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANytE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd07848  161 YVATRWYRSPELLLGAPY-GKAVDMWSVGCILGELSDGQPLFPGES 205
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
53-264 1.94e-28

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: 115.88  E-value: 1.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd07871    7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGgEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-----EFTFGNKL 206
Cdd:cd07871   86 DS-DLKQYLDNCGNlMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARaksvpTKTYSNEV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 207 DTFCGSPPYAapeLFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR 264
Cdd:cd07871  165 VTLWYRPPDV---LLGSTEYSTP-IDMWGVGCILYEMATGRPMFPGSTVKEELHLIFR 218
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
50-267 2.86e-28

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: 114.74  E-value: 2.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMK----EKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNEF 200
Cdd:cd08228   81 LELADAGDLSQMIKYFKKQKrlipERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGlgrfFSSKT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 201 TFGNKLdtfCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPF--DGQNLKELRERVLRGKY 267
Cdd:cd08228  161 TAAHSL---VGTPYYMSPERIHENGYNF-KSDIWSLGCLLYEMAALQSPFygDKMNLFSLCQKIEQCDY 225
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
53-252 3.70e-28

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: 115.21  E-value: 3.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDT-FCG 211
Cdd:cd07846   83 DHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTdYVA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd07846  163 TRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPG 203
AMPKA_C_like cd12120
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and ...
747-839 7.07e-28

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and similar domains; This family is composed of AMPKs, microtubule-associated protein/microtubule affinity regulating kinases (MARKs), yeast Kcc4p-like proteins, plant calcineurin B-Like (CBL)-interacting protein kinases (CIPKs), and similar proteins. They are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. AMPKs act as sensors for the energy status of the cell and are activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. MARKs phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Kcc4p and related proteins are septin-associated proteins that are involved in septin organization and in the yeast morphogenesis checkpoint coordinating the cell cycle with bud formation. CIPKs interact with the calcineurin B-like (CBL) calcium sensors to form a signaling network that decode specific calcium signals triggered by a variety of environmental stimuli including salinity, drought, cold, light, and mechanical perturbation, among others. All members of this family contain an N-terminal catalytic kinase domain and a C-terminal regulatory domain which is also called kinase associated domain 1 (KA1) in some cases. The C-terminal regulatory domain serves as a protein interaction domain in AMPKs and CIPKs. In MARKs and Kcc4p-like proteins, this domain binds phospholipids and may be involved in membrane localization.


Pssm-ID: 213376  Cd Length: 95  Bit Score: 108.02  E-value: 7.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 747 RFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLL-CVHGTP--GHENFVQWEMEVCKLPRlSLNGVRFKRISG 823
Cdd:cd12120    1 RKKWELEIHSRIDPSEIYEGIHKVLEGWGKNLVFRITNFIItGKLVNDhiLFLRSTLFEIEVYEVGP-GLFMVDFKKKTG 79
                         90
                 ....*....|....*.
gi 564332436 824 TSMAFKNIASKIANEL 839
Cdd:cd12120   80 STKTFTKLATKIQIKL 95
MARK4_C cd12197
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
744-841 1.14e-27

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 4; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK4 has two splicing isoforms: MARK4S, predominantly expressed in the brain; and MARK4L, expressed in all tissues. Unlike MARK1-3 that show cytoplasmic localization, MARK4 colocalizes with the centrosome and with microtubules. Decreased MARK4 expression in the brain may be involved in the pathogenesis of Prion diseases and may be correlated to PrP(Sc) deposits. MARK4 is also a component of the ectoplasmic specialization, a testis-specific adherens junction. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213382  Cd Length: 99  Bit Score: 107.30  E-value: 1.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 744 RSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENF-VQWEMEVCKLPRLSLNGVRFKRIS 822
Cdd:cd12197    1 RLLRGGWDVRLRSSRPPAEVVLALREATAGCGCRVRQAGPFLLACLHGAAGSPEPlVAFEAEVCQLPRGELNGVRFKRLW 80
                         90
                 ....*....|....*....
gi 564332436 823 GTSMAFKNIASKIANELKL 841
Cdd:cd12197   81 GTPLAFRTIASKISKELEL 99
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
53-300 1.15e-27

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: 112.40  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREV-RIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVeRHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGgEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCG 211
Cdd:cd14050   83 CDT-SLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKydGPEVDVWSLGV-ILYTLVSGSLPFDGQNLKELRervlrgKYRIP--FY--MSTDCENLLKKFLI 286
Cdd:cd14050  162 DPRYMAPELLQGSF--TKAADIFSLGItILELACNLELPSGGDGWHQLR------QGYLPeeFTagLSPELRSIIKLMMD 233
                        250
                 ....*....|....
gi 564332436 287 LNPSKRGTLEQIMK 300
Cdd:cd14050  234 PDPERRPTAEDLLA 247
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
70-303 1.18e-27

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: 112.44  E-value: 1.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  70 ARHILTGKEVAVKIIDkTQLNSSSLQKLFrevrimKVLNHPNIVKLFEVIETEKTLYLVMEyASGGEVFDYLVAHGRMKE 149
Cdd:cd14022   12 AVHLHSGEELVCKVFD-IGCYQESLAPCF------CLPAHSNINQITEIILGETKAYVFFE-RSYGDMHSFVRTCKKLRE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 150 KEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFC---GSPPYAAPELFQGK-K 225
Cdd:cd14022   84 EEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHDDSLSdkhGCPAYVSPEILNTSgS 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 226 YDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14022  164 YSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
53-300 1.23e-27

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: 113.63  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAI-REASLLKDLKHANIVTLHDIIHTKKTLTLVFEYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGgEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-----EFTFGNKL 206
Cdd:cd07844   81 DT-DLKQYMDDCGGgLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARaksvpSKTYSNEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-QNLKELRERVLR-------------------GK 266
Cdd:cd07844  160 VTLW----YRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRvlgtpteetwpgvssnpefKP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564332436 267 YRIPFY-------------MSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd07844  236 YSFPFYpprplinhaprldRIPHGEELALKFLQYEPKKRISAAEAMK 282
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
53-303 1.27e-27

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: 113.24  E-value: 1.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEA-EDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDTFCG 211
Cdd:cd06641   85 GGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQiKRN*FVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLP--------------------FDGQNLKELRERVLRGKYRIPF 271
Cdd:cd06641  164 TPFWMAPEVIKQSAYDS-KADIWSLGITAIELARGEPPhselhpmkvlflipknnpptLEGNYSKPLKEFVEACLNKEPS 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564332436 272 YMSTDCENLLKKFLILNPSKRGTLEQIMK--DRW 303
Cdd:cd06641  243 FRPTAKELLKHKFILRNAKKTSYLTELIDryKRW 276
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
53-304 1.37e-27

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: 112.75  E-value: 1.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLfREVRIMKVLN------HPNIVKLFEVIETEKTLY 126
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNN--KDYLDQSL-DEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYAsGGEVFDYL-------VAHGRMKekearaKF-RQIVSAVQYCHQKFIVHRDLKAENLLL--DADMNIKIADFGF 196
Cdd:cd14133   78 IVFELL-SQNLYEFLkqnkfqyLSLPRIR------KIaQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 197 SNEFTfgNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYM--- 273
Cdd:cd14133  151 SCFLT--QRLYSYIQSRYYRAPEVILGLPYDEK-IDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMldq 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564332436 274 --STDCE--NLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14133  228 gkADDELfvDFLKKLLEIDPKERPTASQALSHPWL 262
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
57-270 1.40e-27

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: 112.33  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTqLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRET-LPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDT--FCGSP 213
Cdd:cd05084   81 FLTFLRTEGpRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAATggMKQIP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 214 -PYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIP 270
Cdd:cd05084  161 vKWTAPEALNYGRYSS-ESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQG-VRLP 217
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
52-300 1.43e-27

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: 112.32  E-value: 1.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILT-------GKEVAVKIIDKTqlnsSSLQKLFREVRIMKVLN-HPNIVKLFEVIETEK 123
Cdd:cd14019    2 KYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPT----SSPSRILNELECLERLGgSNNVSGLITAFRNED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLvahGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK-IADFGFSNEFTF 202
Cdd:cd14019   78 QVVAVLPYIEHDDFRDFY---RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGvLVDFGLAQREED 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTFC-GSPPYAAPE-LFqgkKY--DGPEVDVWSLGVILYTLVSGSLPF-----DGQNLKELreRVLRGKYripfym 273
Cdd:cd14019  155 RPEQRAPRaGTRGFRAPEvLF---KCphQTTAIDIWSAGVILLSILSGRFPFffssdDIDALAEI--ATIFGSD------ 223
                        250       260
                 ....*....|....*....|....*..
gi 564332436 274 stDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14019  224 --EAYDLLDKLLELDPSKRITAEEALK 248
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
52-299 1.72e-27

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: 112.81  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06646   10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQ--QEIFMVKECKHCNIVAYFGSYLSREKLWICMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFC 210
Cdd:cd06646   88 CGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATiAKRKSFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPE--VDVWSLGVILYTLVSGSLP-FDGQNLKEL----RERVLRGKYRIPFYMSTDCENLLKK 283
Cdd:cd06646  168 GTPYWMAPEVAAVEKNGGYNqlCDIWAVGITAIELAELQPPmFDLHPMRALflmsKSNFQPPKLKDKTKWSSTFHNFVKI 247
                        250
                 ....*....|....*.
gi 564332436 284 FLILNPSKRGTLEQIM 299
Cdd:cd06646  248 SLTKNPKKRPTAERLL 263
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
53-312 2.18e-27

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: 114.05  E-value: 2.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07850    2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEY--ASGGEVFDYLVAHGRMKekearAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNefTFGN 204
Cdd:cd07850   82 LVMELmdANLCQVIQMDLDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 kldTFCGSPP-----YAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-------------------LKELRE 260
Cdd:cd07850  155 ---SFMMTPYvvtryYRAPEVILGMGYK-ENVDIWSVGCIMGEMIRGTVLFPGTDhidqwnkiieqlgtpsdefMSRLQP 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 261 RVL-----RGKYR-IPFYM------------------STDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDE 312
Cdd:cd07850  231 TVRnyvenRPKYAgYSFEElfpdvlfppdseehnklkASQARDLLSKMLVIDPEKRISVDDALQHPYINVWYDPSE 306
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
56-306 2.31e-27

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 112.26  E-value: 2.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIgKGNFAKVKLARHILTGKEVAVKIIDKTQLNssslqklFREV---RIMKvlNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:PHA03390  22 LKLI-DGKFGKVSVLKHKPTQKLFVQKIIKAKNFN-------AIEPmvhQLMK--DNPNFIKLYYSVTTLKGHVLIMDYI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN-IKIADFGFS-NEFTFGnkldTFC 210
Cdd:PHA03390  92 KDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGLCkIIGTPS----CYD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY--RIPF--YMSTDCENLLKKFLI 286
Cdd:PHA03390 168 GTLDYFSPEKIKGHNYD-VSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQqkKLPFikNVSKNANDFVQSMLK 246
                        250       260
                 ....*....|....*....|.
gi 564332436 287 LNPSKR-GTLEQIMKDRWMNV 306
Cdd:PHA03390 247 YNINYRlTNYNEIIKHPFLKI 267
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
53-305 2.42e-27

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 112.99  E-value: 2.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SggevfdyLVAHGRMKEKEARAK--------FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN-IKIADFGFSNEF--- 200
Cdd:PLN00009  84 D-------LDLKKHMDSSPDFAKnprliktyLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARAFgip 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 --TFGNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN-LKEL----------RERVLRGKY 267
Cdd:PLN00009 157 vrTFTHEVVTLW----YRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSeIDELfkifrilgtpNEETWPGVT 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 268 RIPFYMST------------------DCENLLKKFLILNPSKRGTLEQIMKDRWMN 305
Cdd:PLN00009 233 SLPDYKSAfpkwppkdlatvvptlepAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
7-250 3.24e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 114.15  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   7 PLPtlnERDTEQPTLGHLDSKPSSKSNMLRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDK 86
Cdd:PLN00034  33 PLP---QRDPSLAVPLPLPPPSSSSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  87 TQLNSSSLQkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHgrmkEKEARAKFRQIVSAVQYC 166
Cdd:PLN00034 110 NHEDTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIAD----EQFLADVARQILSGIAYL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 167 HQKFIVHRDLKAENLLLDADMNIKIADFGFSNefTFGNKLD---TFCGSPPYAAPE-----LFQGkKYDGPEVDVWSLGV 238
Cdd:PLN00034 185 HRRHIVHRDIKPSNLLINSAKNVKIADFGVSR--ILAQTMDpcnSSVGTIAYMSPErintdLNHG-AYDGYAGDIWSLGV 261
                        250
                 ....*....|..
gi 564332436 239 ILYTLVSGSLPF 250
Cdd:PLN00034 262 SILEFYLGRFPF 273
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
59-266 3.52e-27

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: 112.97  E-value: 3.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDK-TQLNSSSLQKlfREVRIMKVLNHPNIVKLFEVIETEKTLY--LVMEYASGG 135
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDVQM--REFEVLKKLNHKNIVKLFAIEEELTTRHkvLVMELCPCG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLV----AHGrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL----DADMNIKIADFGFSNEFTFGNKLD 207
Cdd:cd13988   79 SLYTVLEepsnAYG-LPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAARELEDDEQFV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332436 208 TFCGSPPYAAPELFQ--------GKKYdGPEVDVWSLGVILYTLVSGSLPF----DGQNLKELRERVLRGK 266
Cdd:cd13988  158 SLYGTEEYLHPDMYEravlrkdhQKKY-GATVDLWSIGVTFYHAATGSLPFrpfeGPRRNKEVMYKIITGK 227
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
50-303 3.64e-27

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: 112.85  E-value: 3.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKII----DKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVIETEK-- 123
Cdd:cd07845    6 VTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVrmdnERDGIPISSL----REITLLLNLRHPNIVELKEVVVGKHld 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASG--GEVFDYLVAhgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFt 201
Cdd:cd07845   82 SIFLVMEYCEQdlASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTY- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 fgnkldtfcGSPP-----------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERV-------- 262
Cdd:cd07845  159 ---------GLPAkpmtpkvvtlwYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIiqllgtpn 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 263 -----------LRGKYRIP----------FYMSTDCE-NLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07845  230 esiwpgfsdlpLVGKFTLPkqpynnlkhkFPWLSEAGlRLLNFLLMYDPKKRATAEEALESSY 292
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
53-238 7.03e-27

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: 110.62  E-value: 7.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS-LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEkWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVfDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNkldTFC 210
Cdd:cd06607   83 CLGSAS-DIVEVHKKpLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPAN---SFV 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 564332436 211 GSPPYAAPELF----QGkKYDGpEVDVWSLGV 238
Cdd:cd06607  159 GTPYWMAPEVIlamdEG-QYDG-KVDVWSLGI 188
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
56-304 8.57e-27

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: 110.92  E-value: 8.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd06642    9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEA-EDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDTFCGSPP 214
Cdd:cd06642   88 SALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQiKRNTFVGTPF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFdgQNLKELR---------ERVLRGKYRIPFymstdcENLLKKFL 285
Cdd:cd06642  167 WMAPEVIKQSAYDF-KADIWSLGITAIELAKGEPPN--SDLHPMRvlflipknsPPTLEGQHSKPF------KEFVEACL 237
                        250
                 ....*....|....*....
gi 564332436 286 ILNPSKRGTLEQIMKDRWM 304
Cdd:cd06642  238 NKDPRFRPTAKELLKHKFI 256
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
55-298 1.30e-26

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: 110.13  E-value: 1.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKV--KLARHILTGK---EVAVKIidkTQLNSSSLQKL--FREVRIMKVLNHPNIVKLFEVIETEKTLYL 127
Cdd:cd05032   10 LIRELGQGSFGMVyeGLAKGVVKGEpetRVAIKT---VNENASMRERIefLNEASVMKEFNCHHVVRLLGVVSTGQPTLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHgRMKEKEA-------RAKF----RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGF 196
Cdd:cd05032   87 VMELMAKGDLKSYLRSR-RPEAENNpglgpptLQKFiqmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 197 ------SNEFTFGNKldtfcGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKY 267
Cdd:cd05032  166 trdiyeTDYYRKGGK-----GLLPvrWMAPESLKDGVFT-TKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLKFVIDGGH 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564332436 268 -RIPfymsTDCENLLKKFLIL----NPSKRGTLEQI 298
Cdd:cd05032  240 lDLP----ENCPDKLLELMRMcwqyNPKMRPTFLEI 271
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
54-270 1.44e-26

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: 110.13  E-value: 1.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKeVAVKIIdktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05072   10 KLVKKLGAGQFGEVWMGYYNNSTK-VAVKTL---KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFTF--GN 204
Cdd:cd05072   86 KGSLLDFLKSDegGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLArviedNEYTAreGA 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 205 KLDTfcgspPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIP 270
Cdd:cd05072  166 KFPI-----KWTAPEAINFGSFT-IKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRG-YRMP 225
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
53-309 1.57e-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: 109.95  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFV---KVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM--NIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14104   79 SGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRgsYIKIIEFGQSRQLKPGDKFRLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PF-YMSTDCENLLKKFL 285
Cdd:cd14104  159 YTSAEFYAPEVHQHESV-STATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFddeAFkNISIEALDFVDRLL 237
                        250       260
                 ....*....|....*....|....
gi 564332436 286 ILNPSKRGTLEQIMKDRWMNVGHE 309
Cdd:cd14104  238 VKERKSRMTAQEALNHPWLKQGME 261
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
53-322 1.80e-26

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: 110.48  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd07873    4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEI-RLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGgEVFDYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-----EFTFGNKL 206
Cdd:cd07873   83 DK-DLKQYLDDCGNSINMHNVKLFLfQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaksipTKTYSNEV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR-------------------GKY 267
Cdd:cd07873  162 VTLW----YRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRilgtpteetwpgilsneefKSY 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 268 RIPFY-----------MSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNvgheddELKPYVEPLPD 322
Cdd:cd07873  238 NYPKYradalhnhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFH------SLGERIHKLPD 297
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
56-341 2.14e-26

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: 109.99  E-value: 2.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05607    7 FRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMaLLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:cd05607   87 GDLKYHIYNVGERGIEMERVIFysAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQRAGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRG------KYRIPFYmSTDCENLLKKFLI 286
Cdd:cd05607  167 NGYMAPEILKEESYSYP-VDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRtledevKFEHQNF-TEEAKDICRLFLA 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 287 LNPSKRgtleqimkdrwMNVGHEDDelkpyveplpdykDPRRTELMVSMGYTREE 341
Cdd:cd05607  245 KKPENR-----------LGSRTNDD-------------DPRKHEFFKSINFPRLE 275
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
50-292 3.49e-26

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: 110.92  E-value: 3.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVL----NHPNIVKLFEVIETEKTL 125
Cdd:cd05633    4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNK 205
Cdd:cd05633   84 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFS-KKK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 206 LDTFCGSPPYAAPELFQ-GKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLK---ELRERVLRGKYRIPFYMSTDCENLL 281
Cdd:cd05633  163 PHASVGTHGYMAPEVLQkGTAYDS-SADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTVNVELPDSFSPELKSLL 241
                        250
                 ....*....|.
gi 564332436 282 KKFLILNPSKR 292
Cdd:cd05633  242 EGLLQRDVSKR 252
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
56-304 3.94e-26

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: 108.99  E-value: 3.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd06640    9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEA-EDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVFDYLVAhGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDTFCGSPP 214
Cdd:cd06640   88 SALDLLRA-GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQiKRNTFVGTPF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPfdGQNLKELRERVLRGKYRIPfYMSTDCENLLKKF----LILNPS 290
Cdd:cd06640  167 WMAPEVIQQSAYDS-KADIWSLGITAIELAKGEPP--NSDMHPMRVLFLIPKNNPP-TLVGDFSKPFKEFidacLNKDPS 242
                        250
                 ....*....|....
gi 564332436 291 KRGTLEQIMKDRWM 304
Cdd:cd06640  243 FRPTAKELLKHKFI 256
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
53-292 3.99e-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: 109.68  E-value: 3.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05632    4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMaLNEKQILEKVNSQFVVNLAYAYETKDALCLVLTI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd05632   84 MNGGDLKFHIYNMGNPGFEEERALFyaAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRE----RVLRGKYRIPFYMSTDCENLLKKFL 285
Cdd:cd05632  164 VGTVGYMAPEVLNNQRY-TLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREevdrRVLETEEVYSAKFSEEAKSICKMLL 242

                 ....*..
gi 564332436 286 ILNPSKR 292
Cdd:cd05632  243 TKDPKQR 249
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
60-299 4.06e-26

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: 107.74  E-value: 4.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  60 GKGNFAKVKLARHILTGKEVAVKiidktqlnssSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFD 139
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK----------KLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 140 YLVAHG--RMKEKEARAKFRQIVSAVQYCHQKF---IVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLdTFCGSPP 214
Cdd:cd14060   72 YLNSNEseEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHM-SLVGTFP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR--IPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd14060  151 WMAPEVIQSLPVS-ETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERptIPSSCPRSFAELMRRCWEADVKER 229

                 ....*..
gi 564332436 293 GTLEQIM 299
Cdd:cd14060  230 PSFKQII 236
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
59-300 4.73e-26

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: 108.29  E-value: 4.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQK-----LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQV-SFCRNSSSEQEevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFGFSNEFT-----FGNKLD 207
Cdd:cd06630   87 GGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGAAARLAskgtgAGEFQG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR-----GKYRIPFYMSTDCENLLK 282
Cdd:cd06630  167 QLLGTIAFMAPEVLRGEQY-GRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKiasatTPPPIPEHLSPGLRDVTL 245
                        250
                 ....*....|....*...
gi 564332436 283 KFLILNPSKRGTLEQIMK 300
Cdd:cd06630  246 RCLELQPEDRPPARELLK 263
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
49-326 5.39e-26

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: 110.09  E-value: 5.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  49 HIG-NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLfREVRIMKVLNHPNIVKLFEVI-----ETE 122
Cdd:cd07849    2 DVGpRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTL-REIKILLRFKHENIIGILDIQrpptfESF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVMEYAsggEVFDY-LVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS---- 197
Cdd:cd07849   81 KDVYIVQELM---ETDLYkLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAriad 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 NEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG----------------------QNL 255
Cdd:cd07849  158 PEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGkdylhqlnlilgilgtpsqedlNCI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 256 KELRER----VLRGKYRIPF-----YMSTDCENLLKKFLILNPSKRGTLEQIMKdrwmnvgHeddelkPYVEPlpdYKDP 326
Cdd:cd07849  238 ISLKARnyikSLPFKPKVPWnklfpNADPKALDLLDKMLTFNPHKRITVEEALA-------H------PYLEQ---YHDP 301
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
53-304 5.54e-26

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: 108.56  E-value: 5.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlfrEVRIMKVL-NHPNIVKLFEV-----IETEKTLY 126
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEA---EYNILKALsDHPNVVKFYGMyykkdVKNGDQLW 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFD----YLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:cd06638   97 LVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GN-KLDTFCGSPPYAAPELFQGKK-----YDGpEVDVWSLGVILYTLVSGSLPFdgQNLKELRE--RVLRG---KYRIPF 271
Cdd:cd06638  177 TRlRRNTSVGTPFWMAPEVIACEQqldstYDA-RCDVWSLGITAIELGDGDPPL--ADLHPMRAlfKIPRNpppTLHQPE 253
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 272 YMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd06638  254 LWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
59-252 5.62e-26

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: 108.20  E-value: 5.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVklARHILTGKEVAVKII--DKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd14146    2 IGVGGFGKV--YRATWKGQEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHGrmKEKEARAKFR-----------QIVSAVQYCHQKFIV---HRDLKAENLLLDADM--------NIKIADF 194
Cdd:cd14146   80 LNRALAAAN--AAPGPRRARRipphilvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIehddicnkTLKITDF 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 195 GFSNEFTFGNKLDTfCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd14146  158 GLAREWHRTTKMSA-AGTYAWMAPEVIKSSLFSKGS-DIWSYGVLLWELLTGEVPYRG 213
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
55-268 5.70e-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: 108.04  E-value: 5.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARhiLTGK-EVAVKIIDKtqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05113    8 FLKELGTGQFGVVKYGK--WRGQyDVAIKMIKE---GSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSnEFTFGNKLDTFCGS 212
Cdd:cd05113   83 NGCLLNYLREMRkRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLS-RYVLDDEYTSSVGS 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332436 213 P---PYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGK--YR 268
Cdd:cd05113  162 KfpvRWSPPEVLMYSKFSS-KSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGLrlYR 222
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
59-300 6.17e-26

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: 107.58  E-value: 6.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIidktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKE----LKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFSNEFTFGNKLD------- 207
Cdd:cd14065   77 ELLKSMDEQLPWSQRVSLaKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKKpdrkkrl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVsGSLPFD----------GQNLKELRERVLRGKYRIPFYMSTDC 277
Cdd:cd14065  157 TVVGSPYWMAPEMLRGESYDE-KVDVFSFGIVLCEII-GRVPADpdylprtmdfGLDVRAFRTLYVPDCPPSFLPLAIRC 234
                        250       260
                 ....*....|....*....|...
gi 564332436 278 ENllkkfliLNPSKRGTLEQIMK 300
Cdd:cd14065  235 CQ-------LDPEKRPSFVELEH 250
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
54-303 6.39e-26

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: 107.84  E-value: 6.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKE---VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05033    7 TIEKVIGGGEFGEVCSGSLKLPGKKeidVAIKTL-KSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN-KLDT 208
Cdd:cd05033   86 YMENGSLDKFLRENdGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEaTYTT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPFYMstDCenllkkfl 285
Cdd:cd05033  166 KGGKIPirWTAPEAIAYRKFT-SASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAVEDG-YRLPPPM--DC-------- 233
                        250
                 ....*....|....*...
gi 564332436 286 ilnPSkrgTLEQIMKDRW 303
Cdd:cd05033  234 ---PS---ALYQLMLDCW 245
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
53-292 6.59e-26

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: 108.54  E-value: 6.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd05631   82 MNGGDLKFHIYNMGNPGFDEQRAIFyaAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYD-GPevDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR------GKYRIPFymSTDCENLLK 282
Cdd:cd05631  162 VGTVGYMAPEVINNEKYTfSP--DWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRrvkedqEEYSEKF--SEDAKSICR 237
                        250
                 ....*....|
gi 564332436 283 KFLILNPSKR 292
Cdd:cd05631  238 MLLTKNPKER 247
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
57-296 6.75e-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: 107.37  E-value: 6.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVklarhiLTGK-----EVAVKIIdKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05034    1 KKLGAGQFGEV------WMGVwngttKVAVKTL-KP--GTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLvahgrmKEKEARAK--------FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----N 198
Cdd:cd05034   72 MSKGSLLDYL------RTGEGRALrlpqlidmAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLArliedD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFTF--GNKLdtfcgspP--YAAPEL-----FQGKKydgpevDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYR 268
Cdd:cd05034  146 EYTAreGAKF-------PikWTAPEAalygrFTIKS------DVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERG-YR 211
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564332436 269 IPfyMSTDCENLLKKFLIL----NPSKRGTLE 296
Cdd:cd05034  212 MP--KPPGCPDELYDIMLQcwkkEPEERPTFE 241
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
52-347 7.81e-26

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: 109.38  E-value: 7.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------ 125
Cdd:cd07855    6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYadfkdv 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-TFGN 204
Cdd:cd07855   86 YVVLDLME-SDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSPE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTF----CGSPPYAAPEL-FQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-------------------LKELR- 259
Cdd:cd07855  165 EHKYFmteyVATRWYRAPELmLSLPEYT-QAIDMWSVGCIFAEMLGRRQLFPGKNyvhqlqliltvlgtpsqavINAIGa 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 260 ERV------LRGKYRIPF---YMSTDCE--NLLKKFLILNPSKRGTLEQIMKDRWMNvGHEDDELKPYVEPLPDYKdprr 328
Cdd:cd07855  244 DRVrryiqnLPNKQPVPWetlYPKADQQalDLLSQMLRFDPSERITVAEALQHPFLA-KYHDPDDEPDCAPPFDFD---- 318
                        330
                 ....*....|....*....
gi 564332436 329 telMVSMGYTREEIQDSLV 347
Cdd:cd07855  319 ---FDAEALTREALKEAIV 334
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
55-252 8.73e-26

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: 107.82  E-value: 8.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVklARHILTGKEVAVKII--DKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd14145   10 LEEIIGIGGFGKV--YRAIWIGDEVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVfDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIV---HRDLKAENLLL-----DADMN---IKIADFGFSNEFT 201
Cdd:cd14145   88 RGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekveNGDLSnkiLKITDFGLAREWH 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564332436 202 FGNKLDTfCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd14145  167 RTTKMSA-AGTYAWMAPEVIRSSMFSKGS-DVWSYGVLLWELLTGEVPFRG 215
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
59-301 8.81e-26

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: 107.48  E-value: 8.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKlaRHILTGKEVAVKI--IDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd14061    2 IGVGGFGKVY--RGIWRGEEVAVKAarQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVahGRMKEKEARAKFR-QIVSAVQYCHQK---FIVHRDLKAENLLLD--------ADMNIKIADFGFSNEFTFGN 204
Cdd:cd14061   80 LNRVLA--GRKIPPHVLVDWAiQIARGMNYLHNEapvPIIHRDLKSSNILILeaienedlENKTLKITDFGLAREWHKTT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTfCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPfyMSTDC----ENL 280
Cdd:cd14061  158 RMSA-AGTYAWMAPEVIKSSTFSKAS-DVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTLP--IPSTCpepfAQL 233
                        250       260
                 ....*....|....*....|.
gi 564332436 281 LKKFLILNPSKRGTLEQIMKD 301
Cdd:cd14061  234 MKDCWQPDPHDRPSFADILKQ 254
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
59-240 9.99e-26

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: 107.59  E-value: 9.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKII----DKTQLNssslqkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELirfdEEAQRN------FLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----------NEFTF 202
Cdd:cd14154   75 GTLKDVLKDMARPLPWAQRVRFaKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgNMSPS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 203 GN----------KLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVIL 240
Cdd:cd14154  155 ETlrhlkspdrkKRYTVVGNPYWMAPEMLNGRSYD-EKVDIFSFGIVL 201
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
50-271 1.01e-25

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: 109.76  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADmLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGF------------ 196
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkkahrtef 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 197 --------SNEFTFGN-----KLDTF-----------CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd05627  161 yrnlthnpPSDFSFQNmnskrKAETWkknrrqlaystVGTPDYIAPEVFMQTGYN-KLCDWWSLGVIMYEMLIGYPPFCS 239
                        250
                 ....*....|....*....
gi 564332436 253 QNLKELRERVLRGKYRIPF 271
Cdd:cd05627  240 ETPQETYRKVMNWKETLVF 258
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
55-301 1.02e-25

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: 108.27  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKE------VAVKIIdKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYL 127
Cdd:cd05053   16 LGKPLGEGAFGQVVKAEAVGLDNKpnevvtVAVKML-KDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHgRMKEKEARA----------KFRQIVS-------AVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05053   95 VVEYASKGNLREFLRAR-RPPGEEASPddprvpeeqlTQKDLVSfayqvarGMEYLASKKCIHRDLAARNVLVTEDNVMK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFS---NEFTFGNKldTFCGSPPYA--APELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRErVLR 264
Cdd:cd05053  174 IADFGLArdiHHIDYYRK--TTNGRLPVKwmAPEALFDRVYT-HQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFK-LLK 249
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564332436 265 GKYRI--PFYMSTDCENLLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd05053  250 EGHRMekPQNCTQELYMLMRDCWHEVPSQRPTFKQLVED 288
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
24-374 1.16e-25

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 110.90  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  24 LDSKPSSKSNMLRGRNSATSADEQPHIGN---------YRLLKTIGKGNFAKVKLARHILTGKEVAVK-IIDKTQLNSss 93
Cdd:PTZ00036  30 MNDKKLDEEERSHNNNAGEDEDEEKMIDNdinrspnksYKLGNIIGNGSFGVVYEAICIDTSEKVAIKkVLQDPQYKN-- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  94 lqklfREVRIMKVLNHPNIVKLFE------VIETEKTLYL--VMEYASGgEVFDYLVAHGRMKEKE----ARAKFRQIVS 161
Cdd:PTZ00036 108 -----RELLIMKNLNHINIIFLKDyyytecFKKNEKNIFLnvVMEFIPQ-TVHKYMKHYARNNHALplflVKLYSYQLCR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 162 AVQYCHQKFIVHRDLKAENLLLDADMN-IKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVIL 240
Cdd:PTZ00036 182 ALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCII 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 241 YTLVSGSLPFDGQN-------------------LKELRERVLRGKY--------RIPFYMST--DCENLLKKFLILNPSK 291
Cdd:PTZ00036 262 AEMILGYPIFSGQSsvdqlvriiqvlgtptedqLKEMNPNYADIKFpdvkpkdlKKVFPKGTpdDAINFISQFLKYEPLK 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 292 RGTLEQIMKDRWMnvghedDELKPYVEPLPDYKDpRRTELmvsMGYTREEIQD-------SLVGQRYNEVMATYLLLGYK 364
Cdd:PTZ00036 342 RLNPIEALADPFF------DDLRDPCIKLPKYID-KLPDL---FNFCDAEIKEmsdacrrKIIPKCTYEAYKEFLMSDEN 411
                        410
                 ....*....|
gi 564332436 365 SSELEGDTIT 374
Cdd:PTZ00036 412 DANIIADKIS 421
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
52-298 1.82e-25

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: 107.27  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLF-----------EVIE 120
Cdd:cd14048    7 DFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRI-RLPNNELAREKVLREVRALAKLDHPGIVRYFnawlerppegwQEKM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 121 TEKTLYLVMEYASGGEVFDYLVAHGRMKEKE---ARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS 197
Cdd:cd14048   86 DEVYLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 N-------EFTFGNKLDTF------CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVsgsLPFDGQNlkelrERVL- 263
Cdd:cd14048  166 TamdqgepEQTVLTPMPAYakhtgqVGTRLYMSPEQIHGNQYS-EKVDIFALGLILFELI---YSFSTQM-----ERIRt 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564332436 264 -----RGKYRIPFYMSTDCEN-LLKKFLILNPSKRGTLEQI 298
Cdd:cd14048  237 ltdvrKLKFPALFTNKYPEERdMVQQMLSPSPSERPEAHEV 277
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
53-254 1.88e-25

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: 106.14  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIID-KTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvRAKKKTSAR----RELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL--DADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd14108   80 CHEELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQYCK 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564332436 210 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd14108  159 YGTPEFVAPEIVNQSPVSK-VTDIWPVGVIAYLCLTGISPFVGEN 202
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
54-254 2.77e-25

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: 105.93  E-value: 2.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLArhILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKvLNHPNIVKLFEvIETEKTL----YLVM 129
Cdd:cd13979    6 RLQEPLGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLA-AETGTDFaslgLIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGG-------EVFDYLVAHGRMKekearaKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:cd13979   82 EYCGNGtlqqliyEGSEPLPLAHRIL------ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 203 GNKLDT----FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd13979  156 GNEVGTprshIGGTYTYRAPELLKGERV-TPKADIYSFGITLWQMLTRELPYAGLR 210
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
53-325 3.23e-25

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: 107.37  E-value: 3.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHI--LTGKEVAVKII--DKTQLNSSSlQKLFREVRIMKVLNHPNIVKLFEVI--ETEKTLY 126
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKFkgDKEQYTGIS-QSACREIALLRELKHENVVSLVEVFleHADKSVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASggevFDYL--VAHGRMKEKEA------RAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN----IKIADF 194
Cdd:cd07842   81 LLFDYAE----HDLWqiIKFHRQAKRVSippsmvKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 195 GFSNefTFGNKLDTFCGSPP------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKElrervlrgKYR 268
Cdd:cd07842  157 GLAR--LFNAPLKPLADLDPvvvtiwYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAKI--------KKS 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 269 IPFYmstdcenllkkflilnpskRGTLEQIMKdrwmNVGHEDDELKPYVEPLPDYKD 325
Cdd:cd07842  227 NPFQ-------------------RDQLERIFE----VLGTPTEKDWPDIKKMPEYDT 260
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
59-195 3.49e-25

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: 101.75  E-value: 3.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTqlNSSSLQKLFREVRIMK-VLNH-PNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDV--NNEEGEDLESEMDILRrLKGLeLNIPKVLVTEDVDGPNILLMELVKGGT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 137 VFDYLVAhGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG 195
Cdd:cd13968   79 LIAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
59-250 3.95e-25

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: 104.88  E-value: 3.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARhiLTGKEVAVKIIDKTQLNssslqklfrEVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14059    1 LGSGAQGAVFLGK--FRGEEVAVKKVRDEKET---------DIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAP 218
Cdd:cd14059   70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGTVAWMAP 149
                        170       180       190
                 ....*....|....*....|....*....|..
gi 564332436 219 ELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd14059  150 EVIRNEPCS-EKVDIWSFGVVLWELLTGEIPY 180
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
52-271 4.01e-25

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: 108.20  E-value: 4.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADmLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG--------------- 195
Cdd:cd05628   82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGlctglkkahrtefyr 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 -----FSNEFTFGN-----KLDTF-----------CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd05628  162 nlnhsLPSDFTFQNmnskrKAETWkrnrrqlafstVGTPDYIAPEVFMQTGYN-KLCDWWSLGVIMYEMLIGYPPFCSET 240
                        250
                 ....*....|....*..
gi 564332436 255 LKELRERVLRGKYRIPF 271
Cdd:cd05628  241 PQETYKKVMNWKETLIF 257
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
53-330 4.90e-25

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: 107.81  E-value: 4.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07876   23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLeefqdvY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEY--ASGGEVFDYLVAHGRMKekearAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN 204
Cdd:cd07876  103 LVMELmdANLCQVIHMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-------------------LKELRERVLRG 265
Cdd:cd07876  178 MMTPYVVTRYYRAPEVILGMGYK-ENVDIWSVGCIMGELVKGSVIFQGTDhidqwnkvieqlgtpsaefMNRLQPTVRNY 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 266 KYRIPFY-----------------------MSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPyvePLPD 322
Cdd:cd07876  257 VENRPQYpgisfeelfpdwifpseserdklKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEA---PPPQ 333

                 ....*...
gi 564332436 323 YKDPRRTE 330
Cdd:cd07876  334 IYDAQLEE 341
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
53-292 1.14e-24

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: 104.74  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKL-FREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKF--RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd05605   82 MNGGDLKFHIYNMGNPGFEEERAVFyaAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR------GKYRIPFymSTDCENLLKK 283
Cdd:cd05605  162 VGTVGYMAPEVVKNERY-TFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRrvkedqEEYSEKF--SEEAKSICSQ 238

                 ....*....
gi 564332436 284 FLILNPSKR 292
Cdd:cd05605  239 LLQKDPKTR 247
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
51-304 1.41e-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: 103.77  E-value: 1.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVK--LARHILTGKEVAVKIIDKtqlnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14112    3 GRFSFGSEIFRGRFSVIVkaVDSTTETDAHCAVKIFEV----SDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 ME--YAsggEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA--DMNIKIADFGFSNEFTfGN 204
Cdd:cd14112   79 MEklQE---DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSvrSWQVKLVDFGRAQKVS-KL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLK--ELRERVLRGKYR---IPFYMSTDCEN 279
Cdd:cd14112  155 GKVPVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDeeETKENVIFVKCRpnlIFVEATQEALR 234
                        250       260
                 ....*....|....*....|....*
gi 564332436 280 LLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14112  235 FATWALKKSPTRRMRTDEALEHRWL 259
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
45-450 1.46e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 110.60  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436   45 DEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFE--VIETE 122
Cdd:PTZ00266    7 DGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDrfLNKAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  123 KTLYLVMEYASGGEVFDYLVA----HGRMKEKEARAKFRQIVSAVQYCHQ-------KFIVHRDLKAENLLLDADMN--- 188
Cdd:PTZ00266   87 QKLYILMEFCDAGDLSRNIQKcykmFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIRhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  189 --------------IKIADFGFSNEFTFGNKLDTFCGSPPYAAPELF--QGKKYDGpEVDVWSLGVILYTLVSGSLPF-D 251
Cdd:PTZ00266  167 kitaqannlngrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSYDD-KSDMWALGCIIYELCSGKTPFhK 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  252 GQNLKELRERVLRGKyRIPFY-MSTDCENLLKKFLILNPSKRGTLEQIMKDRWM-NVG--HEDDELKPYVEPLPDYKDPR 327
Cdd:PTZ00266  246 ANNFSQLISELKRGP-DLPIKgKSKELNILIKNLLNLSAKERPSALQCLGYQIIkNVGppVGAAGGGAGVAAAPGAVVAR 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  328 RTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEG-DTITLKPRPSA-DLTNSSAPSPSHKVQR-----SVS 400
Cdd:PTZ00266  325 RNPSKEHPGLQLAAMEKAKHAEAANYGISPNTLINQRNEEQHGrRSSSCASRQSAnNVTNITSITSVTSVASvasvaSVP 404
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 564332436  401 ANPKQRRSSDQAVPAIPTSNSYSKKTQSNNAENKRPEEETGRKASSTAKV 450
Cdd:PTZ00266  405 SKDDRKYPQDGATHCHAVNGHYGGRVDKDHAERARIEKENAHRKALEMKI 454
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
54-252 1.50e-24

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: 103.96  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVklARHILTGKEVAVKII--DKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd14147    6 RLEEVIGIGGFGKV--YRGSWRGELVAVKAArqDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVahGRMKEKEARAKFR-QIVSAVQYCHQKFIV---HRDLKAENLLLD--------ADMNIKIADFGFSNE 199
Cdd:cd14147   84 AAGGPLSRALA--GRRVPPHVLVNWAvQIARGMHYLHCEALVpviHRDLKSNNILLLqpienddmEHKTLKITDFGLARE 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564332436 200 FTFGNKLDTfCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd14147  162 WHKTTQMSA-AGTYAWMAPEVIKASTF-SKGSDVWSFGVLLWELLTGEVPYRG 212
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
59-277 1.63e-24

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: 104.26  E-value: 1.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKiiDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----------------NEFT 201
Cdd:cd14222   79 DFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekkkpppdkpttKKRT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FG----NKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVsGSLPFDGQNLKELRERVLRGKYRIPFYMSTDC 277
Cdd:cd14222  159 LRkndrKKRYTVVGNPYWMAPEMLNGKSYD-EKVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVRLFWEKFVPKDC 236
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
70-304 1.75e-24

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: 103.03  E-value: 1.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  70 ARHILTGKEVAVKIIdktqlnssSLQKlFREV--RIMKVLNHPNIVKLFEVIETEKTLYLVMEyASGGEVFDYLVAHGRM 147
Cdd:cd14024   12 AEHYQTEKEYTCKVL--------SLRS-YQEClaPYDRLGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 148 KEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFC---GSPPYAAPELFQ-G 223
Cdd:cd14024   82 SEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDDDSLTdkhGCPAYVGPEILSsR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 224 KKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd14024  162 RSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPW 241

                 .
gi 564332436 304 M 304
Cdd:cd14024  242 L 242
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
54-300 1.93e-24

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: 104.24  E-value: 1.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTI---GKGNFAKVKLARHIL----TGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETE--KT 124
Cdd:cd05079    4 RFLKRIrdlGEGHFGKVELCRYDPegdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGGEVFDYL---VAHGRMKEKEARAKfrQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE-- 199
Cdd:cd05079   83 IKLIMEFLPSGSLKEYLprnKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAie 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 -----FTFGNKLDtfcgSPPY-AAPE-LFQGKKYDGPevDVWSLGVILYTLV----SGSLPF----------DGQNLKEL 258
Cdd:cd05079  161 tdkeyYTVKDDLD----SPVFwYAPEcLIQSKFYIAS--DVWSFGVTLYELLtycdSESSPMtlflkmigptHGQMTVTR 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 259 RERVLRGKYRIPfyMSTDC----ENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd05079  235 LVRVLEEGKRLP--RPPNCpeevYQLMRKCWEFQPSKRTTFQNLIE 278
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
140-301 2.04e-24

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: 104.41  E-value: 2.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 140 YLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMN-IKIADFGFSNEFTFGNKL--DTFcGSPPYA 216
Cdd:cd13974  122 YVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLlkDQR-GSPAYI 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 217 APELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF--YMSTDCENLLKKFLILNPSKRGT 294
Cdd:cd13974  201 SPDVLSGKPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRLT 280

                 ....*..
gi 564332436 295 LEQIMKD 301
Cdd:cd13974  281 ASEVLDS 287
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
50-267 2.19e-24

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: 104.34  E-value: 2.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQL-NSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd08229   23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVfDYLVAHGR-----MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNE 199
Cdd:cd08229  103 LELADAGDL-SRMIKHFKkqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGlgrfFSSK 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFGNKLdtfCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPF--DGQNLKELRERVLRGKY 267
Cdd:cd08229  182 TTAAHSL---VGTPYYMSPERIHENGYNF-KSDIWSLGCLLYEMAALQSPFygDKMNLYSLCKKIEQCDY 247
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
56-254 2.41e-24

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: 104.73  E-value: 2.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKT-QLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd06633   26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 gEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNkldTFCGSP 213
Cdd:cd06633  106 -SASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN---SFVGTP 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564332436 214 PYAAPELFQGK---KYDGpEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd06633  182 YWMAPEVILAMdegQYDG-KVDIWSLGITCIELAERKPPLFNMN 224
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
53-325 2.44e-24

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: 105.42  E-value: 2.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhdfY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYAsgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKL 206
Cdd:cd07880   97 LVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTD--SEM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN-LKELRE------------------------- 260
Cdd:cd07880  173 TGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDhLDQLMEimkvtgtpskefvqklqsedaknyv 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 261 ----RVLRGKYRIPF-YMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDElKPYVEPLPDYKD 325
Cdd:cd07880  253 kklpRFRKKDFRSLLpNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPED-ETEAPPYDDSFD 321
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
52-292 2.54e-24

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: 104.74  E-value: 2.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVL----NHPNIVKLFEVIETEKTLYL 127
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLD 207
Cdd:cd14223   81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFS-KKKPH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQ-GKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLK---ELRERVLRGKYRIPFYMSTDCENLLKK 283
Cdd:cd14223  160 ASVGTHGYMAPEVLQkGVAYDS-SADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTMAVELPDSFSPELRSLLEG 238

                 ....*....
gi 564332436 284 FLILNPSKR 292
Cdd:cd14223  239 LLQRDVNRR 247
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
56-311 2.91e-24

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: 103.66  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRI-MKVLNHPNIVKLFEVIETEKTLYLVMEY--A 132
Cdd:cd06617    6 IEELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVmdT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSneftfGNKLDTF- 209
Cdd:cd06617   85 SLDKFYKKVYDKGLTIPEDILGKIAvSIVKALEYLHSKLsVIHRDVKPSNVLINRNGQVKLCDFGIS-----GYLVDSVa 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 ----CGSPPYAAPELFQG----KKYDgPEVDVWSLGVILYTLVSGSLPFD--GQNLKELRERVLRGKYRIP---FymSTD 276
Cdd:cd06617  160 ktidAGCKPYMAPERINPelnqKGYD-VKSDVWSLGITMIELATGRFPYDswKTPFQQLKQVVEEPSPQLPaekF--SPE 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564332436 277 CENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDD 311
Cdd:cd06617  237 FQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKN 271
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
57-301 3.04e-24

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: 102.81  E-value: 3.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLAR-HILTGK--EVAVKIIDKTQLNSSS-LQKLFREVRIMKVLNHPNIVKLFEVIETEKtLYLVMEYA 132
Cdd:cd05040    1 EKLGDGSFGVVRRGEwTTPSGKviQVAVKCLKSDVLSQPNaMDDFLKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLvahgrmkeKEARAKF---------RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----N 198
Cdd:cd05040   80 PLGSLLDRL--------RKDQGHFlistlcdyaVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMralpqN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 E----FTFGNKLdtfcgspPYA--APELFQGKKYDGPEvDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKYRI-- 269
Cdd:cd05040  152 EdhyvMQEHRKV-------PFAwcAPESLKTRKFSHAS-DVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKEGERLer 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564332436 270 PFYMSTDCENLLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd05040  224 PDDCPQDIYNVMLQCWAHKPADRPTFVALRDF 255
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
46-270 3.86e-24

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: 102.51  E-value: 3.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  46 EQPHiGNYRLLKTIGKGNFAKVKLARHiLTGKEVAVKIIdkTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL 125
Cdd:cd05148    2 ERPR-EEFTLERKLGSGYFGEVWEGLW-KNRVRVAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYL-VAHGRMKEKEARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFtfg 203
Cdd:cd05148   78 YIITELMEKGSLLAFLrSPEGQVLPVASLIDMAcQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLI--- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 204 nKLDTFCGSP---PY--AAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIP 270
Cdd:cd05148  155 -KEDVYLSSDkkiPYkwTAPEAASHGTFST-KSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG-YRMP 224
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
94-298 4.83e-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: 102.05  E-value: 4.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  94 LQKLFREVRIMKVLNHPNIVKLFEVIETEKT------LYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCH 167
Cdd:cd14012   42 IQLLEKELESLKKLRHPNLVSYLAFSIERRGrsdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 168 QKFIVHRDLKAENLLLDADM---NIKIADFGFSNEF---TFGNKLDTFcGSPPYAAPELFQGKKYDGPEVDVWSLGVILY 241
Cdd:cd14012  122 RNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLldmCSRGSLDEF-KQTYWLPPELAQGSKSPTRKTDVWDLGLLFL 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 242 TLVSGSLPFdgQNLKELRErvlrgkYRIPFYMSTDCENLLKKFLILNPSKRGTLEQI 298
Cdd:cd14012  201 QMLFGLDVL--EKYTSPNP------VLVSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
57-298 4.87e-24

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: 101.92  E-value: 4.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKeVAVKIIDKTQLnssSLQKLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEYASGGE 136
Cdd:cd14203    1 VKLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTM---SPEAFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLvahgrmKEKEARA--------KFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFTF- 202
Cdd:cd14203   76 LLDFL------KDGEGKYlklpqlvdMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLArliedNEYTAr 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 -GNKLDTFCGSPPYAAPELFQGKKydgpevDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDCENL 280
Cdd:cd14203  150 qGAKFPIKWTAPEAALYGRFTIKS------DVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMP--CPPGCPES 220
                        250       260
                 ....*....|....*....|..
gi 564332436 281 LKKFLI----LNPSKRGTLEQI 298
Cdd:cd14203  221 LHELMCqcwrKDPEERPTFEYL 242
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
52-263 5.33e-24

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: 103.23  E-value: 5.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd07869    6 SYEKLEKLGEGSYATVYKGKSKVNGKLVALKVI-RLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGgEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-----EFTFGNK 205
Cdd:cd07869   85 VHT-DLCQYMDKHpGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARaksvpSHTYSNE 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 206 LDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-QNLKELRERVL 263
Cdd:cd07869  164 VVTLW----YRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmKDIQDQLERIF 218
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
52-300 5.46e-24

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: 102.43  E-value: 5.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEP--GEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFG-NKLDTFC 210
Cdd:cd06645   90 CGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATiAKRKSFI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGPE--VDVWSLGVILYTLVSGSLP-FDGQNLKEL----RERVLRGKYRIPFYMSTDCENLLKK 283
Cdd:cd06645  170 GTPYWMAPEVAAVERKGGYNqlCDIWAVGITAIELAELQPPmFDLHPMRALflmtKSNFQPPKLKDKMKWSNSFHHFVKM 249
                        250
                 ....*....|....*..
gi 564332436 284 FLILNPSKRGTLEQIMK 300
Cdd:cd06645  250 ALTKNPKKRPTAEKLLQ 266
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
59-298 6.64e-24

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: 102.31  E-value: 6.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHilTGKEVAVKIIDK------------TQLNSSSLQ---KLFREVR----IMKVLNHPNIVKLFEVi 119
Cdd:cd14000    2 LGDGGFGSVYRASY--KGEPVAVKIFNKhtssnfanvpadTMLRHLRATdamKNFRLLRqeltVLSHLHHPSIVYLLGI- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 120 eTEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFR----QIVSAVQYCHQKFIVHRDLKAENLLL-----DADMNIK 190
Cdd:cd14000   79 -GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQrialQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFSnEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG----QNLKELRER---VL 263
Cdd:cd14000  158 IADYGIS-RQCCRMGAKGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGhlkfPNEFDIHGGlrpPL 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564332436 264 RGKYRIPFymsTDCENLLKKFLILNPSKRGTLEQI 298
Cdd:cd14000  237 KQYECAPW---PEVEVLMKKCWKENPQQRPTAVTV 268
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
53-292 8.28e-24

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: 102.61  E-value: 8.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSSL---QKLFREVRIMKVLNH-PNIVKLFEVIETEKT---- 124
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEgvpSTALREVSLLQMLSQsIYIVRLLDVEHVEENgkpl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASGgEVFDYLVAHGR-----MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNI-KIADFGFSN 198
Cdd:cd07837   80 LYLVFEYLDT-DLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFTFGNKLDTF-CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-----QNLKELR------ERV---- 262
Cdd:cd07837  159 AFTIPIKSYTHeIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGdselqQLLHIFRllgtpnEEVwpgv 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564332436 263 --LRGKYRIPFYMSTDCE-----------NLLKKFLILNPSKR 292
Cdd:cd07837  239 skLRDWHEYPQWKPQDLSravpdlepegvDLLTKMLAYDPAKR 281
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
31-258 8.31e-24

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: 102.38  E-value: 8.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  31 KSNMLRGRNSATSADeqphigNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlnSSSLQKLFREVRIMKVL-NH 109
Cdd:cd06639    8 NSSMLGLESLADPSD------TWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPI---SDVDEEIEAEYNILRSLpNH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 110 PNIVKLFEVIETEK-----TLYLVMEYASGGEVFDY----LVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAEN 180
Cdd:cd06639   79 PNVVKFYGMFYKADqyvggQLWLVLELCNGGSVTELvkglLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 181 LLLDADMNIKIADFGFSNEFTFGN-KLDTFCGSPPYAAPELFQ-GKKYD---GPEVDVWSLGVILYTLVSGSLP-FDGQN 254
Cdd:cd06639  159 ILLTTEGGVKLVDFGVSAQLTSARlRRNTSVGTPFWMAPEVIAcEQQYDysyDARCDVWSLGITAIELADGDPPlFDMHP 238

                 ....
gi 564332436 255 LKEL 258
Cdd:cd06639  239 VKAL 242
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
59-299 8.49e-24

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: 102.20  E-value: 8.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIV--KLFEVIETEKTLYLVMEYASgGE 136
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVgyHTAWMEHVQLMLYIQMQLCE-LS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHGRMKEKEARAK--------------FRQIVSAVQYCHQKFIVHRDLKAENLLLD-ADMNIKIADFGF----- 196
Cdd:cd14049   93 LWDWIVERNKRPCEEEFKSapytpvdvdvttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLacpdi 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 197 ---SNEFTFGNKLDTF-----CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSgslPFD-----GQNLKELRERVL 263
Cdd:cd14049  173 lqdGNDSTTMSRLNGLthtsgVGTCLYAAPEQLEGSHYD-FKSDMYSIGVILLELFQ---PFGtemerAEVLTQLRNGQI 248
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 264 RGKY--RIPFYMstdceNLLKKFLILNPSKRGTLEQIM 299
Cdd:cd14049  249 PKSLckRWPVQA-----KYIKLLTSTEPSERPSASQLL 281
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
52-298 1.63e-23

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: 100.72  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHilTGKEVAVKIIdKTQLNSsslQKLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEY 131
Cdd:cd05083    7 KLTLGEIIGEGEFGAVLQGEY--MGQKVAVKNI-KCDVTA---QAFLEETAVMTKLQHKNLVRLLGVI-LHNGLYIVMEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARA-KFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGnkLDTF 209
Cdd:cd05083   80 MSKGNLVNFLRSRGRALVPVIQLlQFSlDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMG--VDNS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRI--PFYMSTDCENLLKKFLI 286
Cdd:cd05083  158 RLPVKWTAPEALKNKKFSS-KSDVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAVEKG-YRMepPEGCPPDVYSIMTSCWE 235
                        250
                 ....*....|..
gi 564332436 287 LNPSKRGTLEQI 298
Cdd:cd05083  236 AEPGKRPSFKKL 247
UBA_MARK2 cd14406
UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins; MARK2, also ...
322-363 1.71e-23

UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins; MARK2, also called ELKL motif kinase 1 (EMK-1), MAP/microtubule affinity-regulating kinase 2, PAR1 homolog, or PAR1 homolog b (Par-1b), is enriched in brain. It belongs to the AMPK family of Ser/Thr kinases. MARK2 has been implicated in regulating fertility, immune homeostasis, learning, and memory as well as adiposity, insulin hypersensitivity, and glucose metabolism. The activity of MARK2 is necessary for the outgrowth of cell processes, neurites, and dendritic spines. It is a TORC2 (also known as Crtc2) Ser-275 kinase that blocks TORC2-induced cAMP response element binding protein (CREB) activity. It regulates axon formation via phosphorylation of a kinesin-like motor protein GAKIN/KIF13B. It also acts as a positive regulator of Wnt-beta-catenin signaling.


Pssm-ID: 270589  Cd Length: 42  Bit Score: 93.52  E-value: 1.71e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 564332436 322 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 363
Cdd:cd14406    1 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 42
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
57-292 1.77e-23

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: 100.81  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVK--LARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEkTLYLVMEYASG 134
Cdd:cd05116    1 GELGSGNFGTVKkgYYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAE-SWMLVMEMAEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN---KLDTFCG 211
Cdd:cd05116   80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADEnyyKAQTHGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SP-PYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGK-YRIPFYMSTDCENLLKKFLILN 288
Cdd:cd05116  160 WPvKWYAPECMNYYKFSS-KSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCWTYD 238

                 ....
gi 564332436 289 PSKR 292
Cdd:cd05116  239 VDER 242
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
53-322 1.90e-23

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: 101.99  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd07872    8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGgEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-----EFTFGNKL 206
Cdd:cd07872   87 DK-DLKQYMDDCGNiMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaksvpTKTYSNEV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR-------------------GKY 267
Cdd:cd07872  166 VTLW----YRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRllgtpteetwpgissndefKNY 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 268 RIPFY-----------MSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNvgheddELKPYVEPLPD 322
Cdd:cd07872  242 NFPKYkpqplinhaprLDTEGIELLTKFLQYESKKRISAEEAMKHAYFR------SLGTRIHSLPE 301
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
53-304 2.23e-23

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: 101.29  E-value: 2.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIidkTQLNSS--------SLQKLFREVRIMKVLNHPNIVKLFEVIETEK- 123
Cdd:cd14040    8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKI---HQLNKSwrdekkenYHKHACREYRIHKELDHPRIVKLYDYFSLDTd 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQ--KFIVHRDLKAENLLL---DADMNIKIADFGFS- 197
Cdd:cd14040   85 TFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSk 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 --NEFTFG-NKLDTF---CGSPPYAAPELFQGKKyDGP----EVDVWSLGVILYTLVSGSLPFdGQNLKE---LRERVLR 264
Cdd:cd14040  165 imDDDSYGvDGMDLTsqgAGTYWYLPPECFVVGK-EPPkisnKVDVWSVGVIFFQCLYGRKPF-GHNQSQqdiLQENTIL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564332436 265 GKYRIPF----YMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14040  243 KATEVQFpvkpVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
53-296 2.27e-23

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: 102.47  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07874   19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefqdvY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGG--EVFDYLVAHGRMKekearAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN 204
Cdd:cd07874   99 LVMELMDANlcQVIQMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRgkyripfYMSTDCENLLKKf 284
Cdd:cd07874  174 MMTPYVVTRYYRAPEVILGMGYK-ENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIE-------QLGTPCPEFMKK- 244
                        250
                 ....*....|..
gi 564332436 285 liLNPSKRGTLE 296
Cdd:cd07874  245 --LQPTVRNYVE 254
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
54-247 3.36e-23

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: 100.48  E-value: 3.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHIL----TGKEVAVKIIDKTqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIET--EKTLYL 127
Cdd:cd14205    7 KFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHS--TEEHLRDFEREIEILKSLQHDNIVKYKGVCYSagRRNLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKL 206
Cdd:cd14205   85 IMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEY 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564332436 207 DTF--CGSPP--YAAPELFQGKKYDGPEvDVWSLGVILYTLVSGS 247
Cdd:cd14205  165 YKVkePGESPifWYAPESLTESKFSVAS-DVWSFGVVLYELFTYI 208
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
51-300 3.55e-23

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: 100.95  E-value: 3.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTqlnSSSLQKLFREVRIMKVLNH-PNIVKLFEVI------ETEK 123
Cdd:cd06637    6 GIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVT---GDEEEEIKQEINMLKKYSHhRNIATYYGAFikknppGMDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYL--VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF- 200
Cdd:cd06637   83 QLWLVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLd 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 -TFGNKlDTFCGSPPYAAPELFQGKK-----YDGpEVDVWSLGVILYTLVSGSLPFdgQNLKELRERVLRGKYRIPFYMS 274
Cdd:cd06637  163 rTVGRR-NTFIGTPYWMAPEVIACDEnpdatYDF-KSDLWSLGITAIEMAEGAPPL--CDMHPMRALFLIPRNPAPRLKS 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 275 TDCENLLKKF----LILNPSKRGTLEQIMK 300
Cdd:cd06637  239 KKWSKKFQSFiescLVKNHSQRPSTEQLMK 268
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
56-300 3.57e-23

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: 101.28  E-value: 3.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSS-LQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd06635   30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEkWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 gEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSnefTFGNKLDTFCGSP 213
Cdd:cd06635  110 -SASDLLEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA---SIASPANSFVGTP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGK---KYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYriPFYMSTDCENLLKKF----LI 286
Cdd:cd06635  186 YWMAPEVILAMdegQYDG-KVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNES--PTLQSNEWSDYFRNFvdscLQ 262
                        250
                 ....*....|....
gi 564332436 287 LNPSKRGTLEQIMK 300
Cdd:cd06635  263 KIPQDRPTSEELLK 276
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
55-286 5.79e-23

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: 99.32  E-value: 5.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVklarhiLTGK---EVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVkLFEVIETEKTLYLVMEY 131
Cdd:cd14150    4 MLKRIGTGSFGTV------FRGKwhgDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS---NEFTFGNKLD 207
Cdd:cd14150   77 CEGSSLYRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvkTRWSGSQQVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPPYAAPELFQGKKyDGP---EVDVWSLGVILYTLVSGSLPFDGQNLK-ELRERVLRGkYRIP--FYMSTDCENLL 281
Cdd:cd14150  157 QPSGSILWMAPEVIRMQD-TNPysfQSDVYAYGVVLYELMSGTLPYSNINNRdQIIFMVGRG-YLSPdlSKLSSNCPKAM 234

                 ....*
gi 564332436 282 KKFLI 286
Cdd:cd14150  235 KRLLI 239
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
53-342 7.35e-23

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: 100.88  E-value: 7.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07877   19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefndvY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYAsgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKL 206
Cdd:cd07877   99 LVTHLM--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTD--DEM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN----LK-----------ELRERVLRGKYR--- 268
Cdd:cd07877  175 TGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDhidqLKlilrlvgtpgaELLKKISSESARnyi 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 269 --IPFYMSTDCEN-----------LLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDElKPYVEPLPDYKDPRRTELMVSM 335
Cdd:cd07877  255 qsLTQMPKMNFANvfiganplavdLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDD-EPVADPYDQSFESRDLLIDEWK 333

                 ....*..
gi 564332436 336 GYTREEI 342
Cdd:cd07877  334 SLTYDEV 340
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
50-262 1.00e-22

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: 98.99  E-value: 1.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKE-----VAVKIIDKTqlNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEK 123
Cdd:cd05048    4 LSAVRFLEELGEGAFGKVYKGELLGPSSEesaisVAIKTLKEN--ASPKTQQDFrREAELMSDLQHPNIVCLLGVCTKEQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFR----------------QIVSAVQYCHQKFIVHRDLKAENLLLDADM 187
Cdd:cd05048   82 PQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDgtassldqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDGL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 188 NIKIADFGFSNEFTFGNKLDTFCGSP-P--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERV 262
Cdd:cd05048  162 TVKISDFGLSRDIYSSDYYRVQSKSLlPvrWMPPEAILYGKFT-TESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMI 239
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-320 1.07e-22

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: 98.63  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTgKEVAVKIIdktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05068   11 KLLRKLGSGQFGEVWEGLWNNT-TPVAVKTL---KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:cd05068   87 HGSLLEYLQGKGRSLQLPQLIDMAaQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREGA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 P---PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDCENllkkfliln 288
Cdd:cd05068  167 KfpiKWTAPEAANYNRFS-IKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQVERG-YRMP--CPPNCPP--------- 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564332436 289 pskrgTLEQIMKDRWmnvgHEDDELKPYVEPL 320
Cdd:cd05068  234 -----QLYDIMLECW----KADPMERPTFETL 256
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
55-298 1.42e-22

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: 98.60  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVklARHILTGK-EVAVKIIDKTQLNSSSLqklFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEYAS 133
Cdd:cd05070   13 LIKRLGNGQFGEV--WMGTWNGNtKVAIKTLKPGTMSPESF---LEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLvahgrmKEKEARA--------KFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEF 200
Cdd:cd05070   87 KGSLLDFL------KDGEGRAlklpnlvdMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLArliedNEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TF--GNKLDTFCGSPPYAAPELFQGKKydgpevDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDC 277
Cdd:cd05070  161 TArqGAKFPIKWTAPEAALYGRFTIKS------DVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMP--CPQDC 231
                        250       260
                 ....*....|....*....|....*
gi 564332436 278 ENLLKKFLI----LNPSKRGTLEQI 298
Cdd:cd05070  232 PISLHELMIhcwkKDPEERPTFEYL 256
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
54-272 1.51e-22

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: 98.15  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLK---TIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFE----VIETEKTLY 126
Cdd:cd14033    1 RFLKfniEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDswksTVRGHKCII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF--IVHRDLKAENLLLDADM-NIKIADFGFSNeFTFG 203
Cdd:cd14033   81 LVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGPTgSVKIGDLGLAT-LKRA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 204 NKLDTFCGSPPYAAPELFQgKKYDgPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRGKYRIPFY 272
Cdd:cd14033  160 SFAKSVIGTPEFMAPEMYE-EKYD-EAVDVYAFGMCILEMATSEYPYsECQNAAQIYRKVTSGIKPDSFY 227
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
59-250 1.55e-22

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: 97.75  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVklARHILTGKEVAVKII--DKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd14148    2 IGVGGFGKV--YKGLWRGEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVahGRMKEKEARAKFR-QIVSAVQYCHQKFIV---HRDLKAENLLL--------DADMNIKIADFGFSNEFTFGN 204
Cdd:cd14148   80 LNRALA--GKKVPPHVLVNWAvQIARGMNYLHNEAIVpiiHRDLKSSNILIlepienddLSGKTLKITDFGLAREWHKTT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 205 KLDTfCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPF 250
Cdd:cd14148  158 KMSA-AGTYAWMAPEVIRLSLFSKSS-DVWSFGVLLWELLTGEVPY 201
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
59-303 1.68e-22

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: 98.60  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQlNSSSLQKLFREVRI-MKVLNHPNIVKLFEVIETEKTLYLVMEYASggEV 137
Cdd:cd06618   23 IGSGTCGQVYKMRHKKTGHVMAVKQMRRSG-NKEENKRILMDLDVvLKSHDCPYIVKCYGYFITDSDVFICMELMS--TC 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYLV--AHGRMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPP 214
Cdd:cd06618  100 LDKLLkrIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 215 YAAPELFQGKKYDGPEV--DVWSLGVILYTLVSGSLPFDGQNLK-ELRERVL-----RGKYRIPFymSTDCENLLKKFLI 286
Cdd:cd06618  180 YMAPERIDPPDNPKYDIraDVWSLGISLVELATGQFPYRNCKTEfEVLTKILneeppSLPPNEGF--SPDFCSFVDLCLT 257
                        250
                 ....*....|....*..
gi 564332436 287 LNPSKRGTLEQIMKDRW 303
Cdd:cd06618  258 KDHRYRPKYRELLQHPF 274
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
56-254 1.90e-22

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: 98.94  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKT-QLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd06634   20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 gEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNkldTFCGSP 213
Cdd:cd06634  100 -SASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPAN---SFVGTP 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564332436 214 PYAAPELFQGK---KYDGpEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd06634  176 YWMAPEVILAMdegQYDG-KVDVWSLGITCIELAERKPPLFNMN 218
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
56-318 2.25e-22

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: 98.00  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGG 135
Cdd:cd06622    6 LDELGKGNYGSVYKVLHRPTGVTMAMKEI-RLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 136 EVfDYLVAHGRMKEKEARAKFRQIVSAV-----QYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfGNKLDTFC 210
Cdd:cd06622   85 SL-DKLYAGGVATEGIPEDVLRRITYAVvkglkFLKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV-ASLAKTNI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPPYAAPELFQGKKYDGP-----EVDVWSLGVILYTLVSGSLPFDGQN----LKELRERVLRGKYRIPFYMSTDCENLL 281
Cdd:cd06622  163 GCQSYMAPERIKSGGPNQNptytvQSDVWSLGLSILEMALGRYPYPPETyaniFAQLSAIVDGDPPTLPSGYSDDAQDFV 242
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 282 KKFLILNPSKRGTLEQIMKDRWM-NVGHEDDELKPYVE 318
Cdd:cd06622  243 AKCLNKIPNRRPTYAQLLEHPWLvKYKNADVDMAEWVT 280
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
53-304 2.50e-22

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: 98.59  E-value: 2.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIidkTQLN--------SSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKT 124
Cdd:cd14041    8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKI---HQLNknwrdekkENYHKHACREYRIHKELDHPRIVKLYDYFSLDTD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LY-LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQ--KFIVHRDLKAENLLL---DADMNIKIADFGFSN 198
Cdd:cd14041   85 SFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIKITDFGLSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 --EFTFGNKLDTF------CGSPPYAAPELFQGKKyDGP----EVDVWSLGVILYTLVSGSLPFdGQNLKE---LRERVL 263
Cdd:cd14041  165 imDDDSYNSVDGMeltsqgAGTYWYLPPECFVVGK-EPPkisnKVDVWSVGVIFYQCLYGRKPF-GHNQSQqdiLQENTI 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564332436 264 RGKYRIPF----YMSTDCENLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14041  243 LKATEVQFppkpVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
56-263 2.58e-22

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: 100.09  E-value: 2.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05626    6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDvLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF------------ 202
Cdd:cd05626   86 GDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWthnskyyqkgsh 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 --------------------GNKLDT----------------FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSG 246
Cdd:cd05626  166 irqdsmepsdlwddvsncrcGDRLKTleqratkqhqrclahsLVGTPNYIAPEVLLRKGYT-QLCDWWSVGVILFEMLVG 244
                        250
                 ....*....|....*..
gi 564332436 247 SLPFDGQNLKELRERVL 263
Cdd:cd05626  245 QPPFLAPTPTETQLKVI 261
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
59-240 2.61e-22

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: 97.33  E-value: 2.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKiiDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMK--ELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS----NEFTFGNKLD------ 207
Cdd:cd14221   79 GIIKSMDSHYPWSQRVSFaKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvDEKTQPEGLRslkkpd 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564332436 208 -----TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVIL 240
Cdd:cd14221  159 rkkryTVVGNPYWMAPEMINGRSYD-EKVDVFSFGIVL 195
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
59-249 2.67e-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: 97.51  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLArhiLT--GKEVAVKIIdktQLNSSSL-------QKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd06631    9 LGKGAYGTVYCG---LTstGQLIAVKQV---ELDTSDKekaekeyEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF------- 202
Cdd:cd06631   83 EFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCInlssgsq 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564332436 203 GNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLP 249
Cdd:cd06631  163 SQLLKSMRGTPYWMAPEVINETGH-GRKSDIWSIGCTVFEMATGKPP 208
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
54-265 3.00e-22

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: 96.94  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLArHILTGKEVAVKIIDKTQLnssSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05112    7 TFVQEIGSGQFGLVHLG-YWLNKDKVAIKTIREGAM---SEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSnEFTFGNKLDTFCGS 212
Cdd:cd05112   83 HGCLSDYLRTQrGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMT-RFVLDDQYTSSTGT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 213 P---PYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG 265
Cdd:cd05112  162 KfpvKWSSPEVFSFSRYSS-KSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAG 217
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
59-254 3.13e-22

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: 97.82  E-value: 3.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTqLNSSSLQKLFREVR-IMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGev 137
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKRIRST-VDEKEQKRLLMDLDvVMRSSDCPYIVKFYGALFREGDCWICMELMDIS-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FD--YLVAHGRMKE--------KEARAkfrqIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSneftfGNKL 206
Cdd:cd06616   91 LDkfYKYVYEVLDSvipeeilgKIAVA----TVKALNYLKEELkIIHRDVKPSNILLDRNGNIKLCDFGIS-----GQLV 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 207 DTFC-----GSPPYAAPE-LFQGKKYDGPEV--DVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd06616  162 DSIAktrdaGCRPYMAPErIDPSASRDGYDVrsDVWSLGITLYEVATGKFPYPKWN 217
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
53-356 3.18e-22

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: 98.90  E-value: 3.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEV------IETEKTLY 126
Cdd:cd07851   17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVftpassLEDFQDVY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYAsgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFgnKL 206
Cdd:cd07851   97 LVTHLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDD--EM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN----LKELRE---------------------- 260
Cdd:cd07851  173 TGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDhidqLKRIMNlvgtpdeellkkissesarnyi 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 261 RVLRGKYRIPFY-----MSTDCENLLKKFLILNPSKRGTLEQIMKdrwmnvgHeddelkPYVEPLPDYKDPRRTELM--- 332
Cdd:cd07851  253 QSLPQMPKKDFKevfsgANPLAIDLLEKMLVLDPDKRITAAEALA-------H------PYLAEYHDPEDEPVAPPYdqs 319
                        330       340
                 ....*....|....*....|....*
gi 564332436 333 -VSMGYTREEIQDsLVgqrYNEVMA 356
Cdd:cd07851  320 fESRDLTVDEWKE-LV---YDEIMN 340
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
54-292 3.26e-22

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: 97.58  E-value: 3.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKEVAVKiidktQLNSSSLQK---LFREVRIMKVLN-HPNIVKLF-------EVIETE 122
Cdd:cd14036    3 RIKRVIAEGGFAFVYEAQDVGTGKEYALK-----RLLSNEEEKnkaIIQEINFMKKLSgHPNIVQFCsaasigkEESDQG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVM-EYASGG--EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF--IVHRDLKAENLLLDADMNIKIADFGFS 197
Cdd:cd14036   78 QAEYLLLtELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 --------NEFTFGNKLD-----TFCGSPPYAAPELFQgkKYD----GPEVDVWSLGVILYTLVSGSLPF-DGQNLkelr 259
Cdd:cd14036  158 tteahypdYSWSAQKRSLvedeiTRNTTPMYRTPEMID--LYSnypiGEKQDIWALGCILYLLCFRKHPFeDGAKL---- 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 260 eRVLRGKYRIPfymSTDCE-----NLLKKFLILNPSKR 292
Cdd:cd14036  232 -RIINAKYTIP---PNDTQytvfhDLIRSTLKVNPEER 265
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
53-296 3.90e-22

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: 98.96  E-value: 3.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07875   26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefqdvY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEY--ASGGEVFDYLVAHGRMKekearAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN 204
Cdd:cd07875  106 IVMELmdANLCQVIQMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRgkyripfYMSTDCENLLKKf 284
Cdd:cd07875  181 MMTPYVVTRYYRAPEVILGMGYK-ENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIE-------QLGTPCPEFMKK- 251
                        250
                 ....*....|..
gi 564332436 285 liLNPSKRGTLE 296
Cdd:cd07875  252 --LQPTVRTYVE 261
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
52-296 3.95e-22

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: 96.88  E-value: 3.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKeVAVKIIDKtqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEY 131
Cdd:cd05067    8 TLKLVERLGAGQFGEVWMGYYNGHTK-VAIKSLKQ---GSMSPDAFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARA--KFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFTF-- 202
Cdd:cd05067   83 MENGSLVDFLKTPSGIKLTINKLldMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLArliedNEYTAre 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 GNKLDTfcgspPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDCE--- 278
Cdd:cd05067  163 GAKFPI-----KWTAPEAINYGTFT-IKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLERG-YRMP--RPDNCPeel 233
                        250
                 ....*....|....*....
gi 564332436 279 -NLLKKFLILNPSKRGTLE 296
Cdd:cd05067  234 yQLMRLCWKERPEDRPTFE 252
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
53-321 4.30e-22

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: 98.31  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI-----ETEKTLYL 127
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYAsGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLD 207
Cdd:cd07859   82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TF----CGSPPYAAPEL---FQGkKYDgPEVDVWSLGVILYTLVSGSLPFDGQNL---------------KELRERV--- 262
Cdd:cd07859  161 IFwtdyVATRWYRAPELcgsFFS-KYT-PAIDIWSIGCIFAEVLTGKPLFPGKNVvhqldlitdllgtpsPETISRVrne 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332436 263 --------LRGKYRIPF---YMSTD--CENLLKKFLILNPSKRGTLEQIMKDRWMNvGHEDDELKPYVEPLP 321
Cdd:cd07859  239 karrylssMRKKQPVPFsqkFPNADplALRLLERLLAFDPKDRPTAEEALADPYFK-GLAKVEREPSAQPIT 309
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
51-250 5.75e-22

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: 97.00  E-value: 5.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlfrEVRIMKVLNHPNIVKLFEVIETEKT------ 124
Cdd:cd06636   16 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKL---EINMLKKYSHHRNIATYYGAFIKKSppghdd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 -LYLVMEYASGGEVFDyLVAHGR---MKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF 200
Cdd:cd06636   93 qLWLVMEFCGAGSVTD-LVKNTKgnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 201 --TFGNKlDTFCGSPPYAAPELFQGKK-----YDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd06636  172 drTVGRR-NTFIGTPYWMAPEVIACDEnpdatYD-YRSDIWSLGITAIEMAEGAPPL 226
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
53-259 5.76e-22

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: 96.72  E-value: 5.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHI-LTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVL---NHPNIVKLFEVIETEKTLYLV 128
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYL---VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK 205
Cdd:cd14052   82 TELCENGSLDVFLselGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLIRG 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 206 LDTFcGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSG-SLPFDGQNLKELR 259
Cdd:cd14052  162 IERE-GDREYIAPEILSEHMYDKP-ADIFSLGLILLEAAANvVLPDNGDAWQKLR 214
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
59-298 6.17e-22

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: 96.17  E-value: 6.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVklARHILTGKEVAVKIIDKtqlnSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLylVMEYASGGEVf 138
Cdd:cd14068    2 LGDGGFGSV--YRAVYRGEDVAVKIFNK----HTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKGSL- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL-----DADMNIKIADFGFSnEFTFGNKLDTFCG 211
Cdd:cd14068   73 DALLQQdnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIA-QYCCRMGIKTSEG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVS-GSLPFDGQNL-KELRERVLRGKYRIPFyMSTDC------ENLLKK 283
Cdd:cd14068  152 TPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTcGERIVEGLKFpNEFDELAIQGKLPDPV-KEYGCapwpgvEALIKD 230
                        250
                 ....*....|....*
gi 564332436 284 FLILNPSKRGTLEQI 298
Cdd:cd14068  231 CLKENPQCRPTSAQV 245
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
52-284 7.00e-22

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: 95.99  E-value: 7.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKiIDKTQLNSSSLQklfREVRIMKVLN-HPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSKHPQLE---YEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YAsGGEVFDYLVAHGRmkekearaKF---------RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK---IADFGFSN 198
Cdd:cd14016   77 LL-GPSLEDLFNKCGR--------KFslktvlmlaDQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFtfgnkLDTFCGS-PPYAapelfQGKK------Y--------------DgpevDVWSLG-VILYtLVSGSLPFDG---Q 253
Cdd:cd14016  148 KY-----RDPRTGKhIPYR-----EGKSltgtarYasinahlgieqsrrD----DLESLGyVLIY-FLKGSLPWQGlkaQ 212
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564332436 254 NLKELRERVLRGKyripfyMSTD----CENLLKKF 284
Cdd:cd14016  213 SKKEKYEKIGEKK------MNTSpeelCKGLPKEF 241
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
53-324 7.03e-22

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: 97.64  E-value: 7.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEV-IETEKTLYLVMEY 131
Cdd:cd07856   12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVTEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 AsgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNefTFGNKLDTFCG 211
Cdd:cd07856   92 L--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR--IQDPQMTGYVS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 SPPYAAPE-LFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-------LKEL-------------RERVLR------ 264
Cdd:cd07856  168 TRYYRAPEiMLTWQKYD-VEVDIWSAGCIFAEMLEGKPLFPGKDhvnqfsiITELlgtppddvinticSENTLRfvqslp 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 265 GKYRIPFY-----MSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEddelkPYVEPLPDYK 324
Cdd:cd07856  247 KRERVPFSekfknADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHD-----PTDEPVADEK 306
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
54-245 7.77e-22

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: 96.51  E-value: 7.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTI---GKGNFAKVKLARHIL----TGKEVAVKII--DKTQLNSSSLQKlfrEVRIMKVLNHPNIVKLFEVIET--E 122
Cdd:cd05080    4 RYLKKIrdlGEGHFGKVSLYCYDPtndgTGEMVAVKALkaDCGPQHRSGWKQ---EIDILKTLYHENIVKYKGCCSEqgG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVMEYASGGEVFDYLVAHgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:cd05080   81 KSLQLIMEYVPLGSLRDYLPKH-SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564332436 203 GNKLDTFC--GSPP--YAAPELFQGKKYDGPEvDVWSLGVILYTLVS 245
Cdd:cd05080  160 GHEYYRVRedGDSPvfWYAPECLKEYKFYYAS-DVWSFGVTLYELLT 205
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
55-301 1.06e-21

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: 96.62  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKE-------VAVKIIdKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLY 126
Cdd:cd05098   17 LGKPLGEGCFGQVVLAEAIGLDKDkpnrvtkVAVKML-KSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYL----------------VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05098   96 VIVEYASKGNLREYLqarrppgmeycynpshNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFSNEFtfgNKLD----TFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELReRVL 263
Cdd:cd05098  176 IADFGLARDI---HHIDyykkTTNGRLPvkWMAPEALFDRIYTH-QSDVWSFGVLLWEIFTlGGSPYPGVPVEELF-KLL 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564332436 264 RGKYRIPfyMSTDCENLLkkFLILN------PSKRGTLEQIMKD 301
Cdd:cd05098  251 KEGHRMD--KPSNCTNEL--YMMMRdcwhavPSQRPTFKQLVED 290
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
57-307 1.34e-21

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: 97.51  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETE-----KTLYLVMEY 131
Cdd:cd07853    6 RPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPhidpfEEIYVVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGgEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN--EFTFGNKLDTF 209
Cdd:cd07853   86 MQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARveEPDESKHMTQE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN-LKEL----------------------RERVLRGK 266
Cdd:cd07853  165 VVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSpIQQLdlitdllgtpsleamrsacegaRAHILRGP 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564332436 267 YRIP-----FYMSTDCE----NLLKKFLILNPSKRGTLEQIMKDRWMNVG 307
Cdd:cd07853  245 HKPPslpvlYTLSSQATheavHLLCRMLVFDPDKRISAADALAHPYLDEG 294
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
51-306 1.36e-21

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 97.16  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlnSSSLQKLFREVRIMKVLNHPNIVKLFEVI----------- 119
Cdd:cd07854    5 SRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTD--PQSVKHALREIKIIRRLDHDNIVKVYEVLgpsgsdltedv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 120 --ETE-KTLYLVMEYASGGevFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDA-DMNIKIADFG 195
Cdd:cd07854   83 gsLTElNSVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTeDLVLKIGDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 FSN----EFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR------- 264
Cdd:cd07854  161 LARivdpHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILEsvpvvre 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 265 ------------------GKYRIPF---YMSTDCE--NLLKKFLILNPSKRGTLEQIMKDRWMNV 306
Cdd:cd07854  241 edrnellnvipsfvrndgGEPRRPLrdlLPGVNPEalDFLEQILTFNPMDRLTAEEALMHPYMSC 305
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
55-298 1.69e-21

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: 95.18  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKE---VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIEtEKTLYLVMEY 131
Cdd:cd05056   10 LGRCIGEGQFGDVYQGVYMSPENEkiaVAVKTC-KNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT-ENPVWIVMEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFC 210
Cdd:cd05056   88 APLGELRSYLQVNKYSLDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 GSPP--YAAPELFQGKKYDGPEvDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKyRIPfyMSTDCE----NLLKK 283
Cdd:cd05056  168 GKLPikWMAPESINFRRFTSAS-DVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGE-RLP--MPPNCPptlySLMTK 243
                        250
                 ....*....|....*
gi 564332436 284 FLILNPSKRGTLEQI 298
Cdd:cd05056  244 CWAYDPSKRPRFTEL 258
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
59-257 2.58e-21

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: 94.38  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLAR-HiltgKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVkLFEVIETEKTLYLVMEYASGGEV 137
Cdd:cd14062    1 IGSGSFGTVYKGRwH----GDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGSSL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 138 FDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF---CGSP 213
Cdd:cd14062   76 YKHLhVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFeqpTGSI 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 214 PYAAPELF--QGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKE 257
Cdd:cd14062  156 LWMAPEVIrmQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
52-252 2.95e-21

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: 95.03  E-value: 2.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd07870    1 SYLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTFVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGgEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEF-----TFGNK 205
Cdd:cd07870   80 MHT-DLAQYMIQHpGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKsipsqTYSSE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564332436 206 LDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG 252
Cdd:cd07870  159 VVTLW----YRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
53-319 2.95e-21

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: 96.27  E-value: 2.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEV------IETEKTLY 126
Cdd:cd07878   17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVftpatsIENFNEVY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYAsgGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKL 206
Cdd:cd07878   97 LVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQAD--DEM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR------------------GKY- 267
Cdd:cd07878  173 TGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEvvgtpspevlkkissehaRKYi 252
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 268 -RIPFYMSTDCE-----------NLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDElKPYVEP 319
Cdd:cd07878  253 qSLPHMPQQDLKkifrganplaiDLLEKMLVLDSDKRISASEALAHPYFSQYHDPED-EPEAEP 315
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
52-301 3.97e-21

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: 94.64  E-value: 3.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKV--KLARHI--LTG-KEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLY 126
Cdd:cd05045    1 NLVLGKTLGEGEFGKVvkATAFRLkgRAGyTTVAVKML-KENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYL-----VAHGRMKEKEARAKFR-------------------QIVSAVQYCHQKFIVHRDLKAENLL 182
Cdd:cd05045   80 LIVEYAKYGSLRSFLresrkVGPSYLGSDGNRNSSYldnpderaltmgdlisfawQISRGMQYLAEMKLVHRDLAARNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 183 LDADMNIKIADFGFSNE-FTFGNKLDTFCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDG---QNL 255
Cdd:cd05045  160 VAEGRKMKISDFGLSRDvYEEDSYVKRSKGRIPvkWMAIESLFDHIYT-TQSDVWSFGVLLWEIVTlGGNPYPGiapERL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 256 KELrervLRGKYRI--PFYMSTDCENLLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd05045  239 FNL----LKTGYRMerPENCSEEMYNLMLTCWKQEPDKRPTFADISKE 282
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
53-240 4.09e-21

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: 94.64  E-value: 4.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQ-KLFREVRIMKVL---NHPNIVKLFEVIETEKT---- 124
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSV-RVQTNEDGLPlSTVREVALLKRLeafDHPNIVRLMDVCATSRTdret 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 -LYLVMEYASGgEVFDYL--VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT 201
Cdd:cd07863   81 kVTLVFEHVDQ-DLRTYLdkVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYS 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564332436 202 FGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVIL 240
Cdd:cd07863  160 CQMALTPVVVTLWYRAPEVLLQSTYATP-VDMWSVGCIF 197
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
51-265 4.54e-21

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: 93.97  E-value: 4.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVklarhiLTGK---EVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVkLFEVIETEKTLYL 127
Cdd:cd14151    8 GQITVGQRIGSGSFGTV------YKGKwhgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS---NEFTFG 203
Cdd:cd14151   81 VTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkSRWSGS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 204 NKLDTFCGSPPYAAPEL--FQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-QNLKELRERVLRG 265
Cdd:cd14151  161 HQFEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRG 225
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
54-299 6.02e-21

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: 93.63  E-value: 6.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLK---TIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFE----VIETEKTLY 126
Cdd:cd14031   10 RFLKfdiELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDswesVLKGKKCIV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF--IVHRDLKAENLLLDADM-NIKIADFGFSN--EFT 201
Cdd:cd14031   90 LVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATlmRTS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNKLdtfCGSPPYAAPELFQgKKYDgPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRGKYRIPFYMSTDCE-- 278
Cdd:cd14031  170 FAKSV---IGTPEFMAPEMYE-EHYD-ESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTSGIKPASFNKVTDPEvk 244
                        250       260
                 ....*....|....*....|.
gi 564332436 279 NLLKKFLILNPSKRGTLEQIM 299
Cdd:cd14031  245 EIIEGCIRQNKSERLSIKDLL 265
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
55-300 1.47e-20

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: 93.49  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKE-------VAVKIIdKTQLNSSSLQKLFREVRIMKVLN-HPNIVKLFEVIETEKTLY 126
Cdd:cd05099   16 LGKPLGEGCFGQVVRAEAYGIDKSrpdqtvtVAVKML-KDNATDKDLADLISEMELMKLIGkHKNIINLLGVCTQEGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAH---------GRMKEKEARAKFRQIVSAV-------QYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05099   95 VIVEYAAKGNLREFLRARrppgpdytfDITKVPEEQLSFKDLVSCAyqvargmEYLESRRCIHRDLAARNVLVTEDNVMK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFS---NEFTFGNKldTFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELReRVLR 264
Cdd:cd05099  175 IADFGLArgvHDIDYYKK--TSNGRLPvkWMAPEALFDRVYTH-QSDVWSFGILMWEIFTlGGSPYPGIPVEELF-KLLR 250
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 265 GKYRI--PFYMSTDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd05099  251 EGHRMdkPSNCTHELYMLMRECWHAVPTQRPTFKQLVE 288
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
54-303 1.52e-20

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: 92.24  E-value: 1.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKE---VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05066    7 KIEKVIGAGEFGEVCSGRLKLPGKReipVAIKTL-KAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN--EFTFGNKLD 207
Cdd:cd05066   86 YMENGSLDAFLRKHdGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDPEAAYT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPP--YAAPELFQGKKYDGPEvDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPFYMstDCEnllkkf 284
Cdd:cd05066  166 TRGGKIPirWTAPEAIAYRKFTSAS-DVWSYGIVMWEVMSyGERPYWEMSNQDVIKAIEEG-YRLPAPM--DCP------ 235
                        250
                 ....*....|....*....
gi 564332436 285 lilnpskrGTLEQIMKDRW 303
Cdd:cd05066  236 --------AALHQLMLDCW 246
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
59-300 1.87e-20

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: 91.61  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSslqklfrEVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS-------DVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLdadMNIK--IADFGFSNEFT----FGNKLDtfcGS 212
Cdd:cd13995   85 EKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF---MSTKavLVDFGLSVQMTedvyVPKDLR---GT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 PPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFdgqnlkelRERVLRGKYriPFYM-----------------ST 275
Cdd:cd13995  159 EIYMSPEVILCRGHN-TKADIYSLGATIIHMQTGSPPW--------VRRYPRSAY--PSYLyiihkqapplediaqdcSP 227
                        250       260
                 ....*....|....*....|....*
gi 564332436 276 DCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd13995  228 AMRELLEAALERNPNHRSSAAELLK 252
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
59-254 2.51e-20

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 91.79  E-value: 2.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVieTEKTLYLVMEYASGGEVF 138
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGI--CSEPVGLVMEYMETGSLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKearaKFRQI-VSAVQ----YCHQKFIVHRDLKAENLLLDADMNIKIADFGFS--NEFTFGNKL--DTF 209
Cdd:cd14025   82 KLLASEPLPWEL----RFRIIhETAVGmnflHCMKPPLLHLDLKPANILLDAHYHVKISDFGLAkwNGLSHSHDLsrDGL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 210 CGSPPYAAPELF-QGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd14025  158 RGTIAYLPPERFkEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGEN 203
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
55-245 2.76e-20

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: 91.76  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLA--RHILTGKE---VAVKIIDKTqlNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd05049    9 LKRELGEGAFGKVFLGecYNLEPEQDkmlVAVKTLKDA--SSPDARKDFeREAELLTNLQHENIVKFYGVCTEGDPLLMV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHG---RMKEKEARAKFR-----------QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADF 194
Cdd:cd05049   87 FEYMEHGDLNKFLRSHGpdaAFLASEDSAPGEltlsqllhiavQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDF 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 195 GFSNEfTFGNKLDTFCGSP--P--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS 245
Cdd:cd05049  167 GMSRD-IYSTDYYRVGGHTmlPirWMPPESILYRKFT-TESDVWSFGVVLWEIFT 219
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
52-298 3.64e-20

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: 92.16  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKE-----VAVKIIdKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTL 125
Cdd:cd05055   36 NLSFGKTLGAGAFGKVVEATAYGLSKSdavmkVAVKML-KPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYLvahgrMKEKEARAKFR-------QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS- 197
Cdd:cd05055  115 LVITEYCCYGDLLNFL-----RRKRESFLTLEdllsfsyQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLAr 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 ---NEFTFGNKLDTFCgsP-PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKYRI--P 270
Cdd:cd05055  190 dimNDSNYVVKGNARL--PvKWMAPESIFNCVYT-FESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMaqP 266
                        250       260
                 ....*....|....*....|....*...
gi 564332436 271 FYMSTDCENLLKKFLILNPSKRGTLEQI 298
Cdd:cd05055  267 EHAPAEIYDIMKTCWDADPLKRPTFKQI 294
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
54-270 4.17e-20

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: 91.32  E-value: 4.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGK----EVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEkTLYLVM 129
Cdd:cd05057   10 EKGKVLGSGAFGTVYKGVWIPEGEkvkiPVAIKVL-REETGPKANEEILDEAYVMASVDHPHLVRLLGICLSS-QVQLIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK-LD 207
Cdd:cd05057   88 QLMPLGCLLDYVRNHrDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKeYH 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 208 TFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKyRIP 270
Cdd:cd05057  168 AEGGKVPikWMALESIQYRIYTH-KSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGE-RLP 231
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
59-250 4.33e-20

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: 90.67  E-value: 4.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHilTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLF-EVIETEKTLYLVMEYASGGE 136
Cdd:cd14064    1 IGSGSFGKVYKGRC--RNKIVAIKRYRANTYCSKSDVDMFcREVSILCRLNHPCVIQFVgACLDDPSQFAIVTQYVSGGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLvaHGRMKEKEARAKFR---QIVSAVQYCHQ--KFIVHRDLKAENLLLDADMNIKIADFGFSnEFTFGNKLDTFCG 211
Cdd:cd14064   79 LFSLL--HEQKRVIDLQSKLIiavDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGES-RFLQSLDEDNMTK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564332436 212 SPP---YAAPELF-QGKKYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd14064  156 QPGnlrWMAPEVFtQCTRYS-IKADVFSYALCLWELLTGEIPF 197
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
55-301 4.41e-20

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: 92.00  E-value: 4.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKE-------VAVKIIdKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLY 126
Cdd:cd05101   28 LGKPLGEGCFGQVVMAEAVGIDKDkpkeavtVAVKML-KDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYL----------------VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05101  107 VIVEYASKGNLREYLrarrppgmeysydinrVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMK 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFSNEFtfgNKLD----TFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELReRVL 263
Cdd:cd05101  187 IADFGLARDI---NNIDyykkTTNGRLPvkWMAPEALFDRVYTH-QSDVWSFGVLMWEIFTlGGSPYPGIPVEELF-KLL 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564332436 264 RGKYRIP---------FYMSTDCENLLkkflilnPSKRGTLEQIMKD 301
Cdd:cd05101  262 KEGHRMDkpanctnelYMMMRDCWHAV-------PSQRPTFKQLVED 301
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
56-264 5.28e-20

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 93.19  E-value: 5.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQ-LNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05625    6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG------------------- 195
Cdd:cd05625   86 GDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdh 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 -------FSNEF------TFGNKLD----------------TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSG 246
Cdd:cd05625  166 lrqdsmdFSNEWgdpencRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVG 244
                        250
                 ....*....|....*...
gi 564332436 247 SLPFDGQNLKELRERVLR 264
Cdd:cd05625  245 QPPFLAQTPLETQMKVIN 262
pknD PRK13184
serine/threonine-protein kinase PknD;
50-356 6.00e-20

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 95.61  E-value: 6.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  50 IGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFlREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGgEVFDYLVAHGRMKE---KEARAK---------FRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG- 195
Cdd:PRK13184  81 MPYIEG-YTLKSLLKSVWQKEslsKELAEKtsvgaflsiFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGa 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 ---------------------FSNEFTFGNKLdtfCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPF---D 251
Cdd:PRK13184 160 aifkkleeedlldidvderniCYSSMTIPGKI---VGTPDYMAPERLLGVPAS-ESTDIYALGVILYQMLTLSFPYrrkK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 252 GQNLKeLRERVLR----GKYR-IPFYMStdceNLLKKFLILNPskrgtleqimKDRWMNVGHEDDELKPYVEplpdyKDP 326
Cdd:PRK13184 236 GRKIS-YRDVILSpievAPYReIPPFLS----QIAMKALAVDP----------AERYSSVQELKQDLEPHLQ-----GSP 295
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564332436 327 RRTELMVSMGYTRE--EIQDSLVGQRYNEVMA 356
Cdd:PRK13184 296 EWTVKATLMTKKKScwKFYEPILLSKYFPMLE 327
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
55-265 7.55e-20

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: 89.92  E-value: 7.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKeVAVKIIDKtqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05114    8 FMKELGSGLFGVVRLGKWRAQYK-VAIKAIRE---GAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLvahgrmkeKEARAKFRQ---------IVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSnEFTFGNK 205
Cdd:cd05114   84 GCLLNYL--------RQRRGKLSRdmllsmcqdVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT-RYVLDDQ 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 206 LDTFCGSP---PYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG 265
Cdd:cd05114  155 YTSSSGAKfpvKWSPPEVFNYSKFSS-KSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRG 217
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
54-298 7.93e-20

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: 90.52  E-value: 7.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKeVAVKIIDKTQLnssSLQKLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEYAS 133
Cdd:cd05069   15 RLDVKLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTM---MPEAFLQEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLvahgrmkeKEARAKF----------RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----N 198
Cdd:cd05069   90 KGSLLDFL--------KEGDGKYlklpqlvdmaAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLArliedN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 199 EFTF--GNKLDTFCGSPPYAAPELFQGKKydgpevDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMST 275
Cdd:cd05069  162 EYTArqGAKFPIKWTAPEAALYGRFTIKS------DVWSFGILLTELVTkGRVPYPGMVNREVLEQVERG-YRMP--CPQ 232
                        250       260
                 ....*....|....*....|....*..
gi 564332436 276 DCENLLKKFLIL----NPSKRGTLEQI 298
Cdd:cd05069  233 GCPESLHELMKLcwkkDPDERPTFEYI 259
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
55-323 8.60e-20

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: 91.62  E-value: 8.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARHILTGKE-------VAVKIIdKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLY 126
Cdd:cd05100   16 LGKPLGEGCFGQVVMAEAIGIDKDkpnkpvtVAVKML-KDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAH---------GRMKEKEARAKFRQIVS-------AVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05100   95 VLVEYASKGNLREYLRARrppgmdysfDTCKLPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVMK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGFSNEFtfgNKLD----TFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELReRVL 263
Cdd:cd05100  175 IADFGLARDV---HNIDyykkTTNGRLPvkWMAPEALFDRVYTH-QSDVWSFGVLLWEIFTlGGSPYPGIPVEELF-KLL 249
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 264 RGKYRI--PFYMSTDCENLLKKFLILNPSKRGTLEQIMK--DRWMNVGHEDDELKPYVePLPDY 323
Cdd:cd05100  250 KEGHRMdkPANCTHELYMIMRECWHAVPSQRPTFKQLVEdlDRVLTVTSTDEYLDLSV-PFEQY 312
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
76-300 9.28e-20

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: 90.02  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  76 GKEVAVKIIdktqlnsssLQKLF----REVrimKVL----NHPNIVKLFEVIETEKTLYLVMEY--ASGGEVFDYLVAHG 145
Cdd:cd13982   25 GRPVAVKRL---------LPEFFdfadREV---QLLresdEHPNVIRYFCTEKDRQFLYIALELcaASLQDLVESPRESK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 146 RMKEKEARAK--FRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-----MNIKIADFGFS-----NEFTFGNkLDTFCGSP 213
Cdd:cd13982   93 LFLRPGLEPVrlLRQIASGLAHLHSLNIVHRDLKPQNILISTPnahgnVRAMISDFGLCkkldvGRSSFSR-RSGVAGTS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 214 PYAAPELFQGKKYDGP--EVDVWSLG-VILYTLVSGSLPFdGQNLKelRER-VLRGKYRIPFYMS-----TDCENLLKKF 284
Cdd:cd13982  172 GWIAPEMLSGSTKRRQtrAVDIFSLGcVFYYVLSGGSHPF-GDKLE--REAnILKGKYSLDKLLSlgehgPEAQDLIERM 248
                        250
                 ....*....|....*.
gi 564332436 285 LILNPSKRGTLEQIMK 300
Cdd:cd13982  249 IDFDPEKRPSAEEVLN 264
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
54-296 9.84e-20

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: 90.09  E-value: 9.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKeVAVKIIdktQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEYAS 133
Cdd:cd05073   14 KLEKKLGAGQFGEVWMATYNKHTK-VAVKTM---KPGSMSVEAFLAEANVMKTLQHDKLVKLHAVV-TKEPIYIITEFMA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVA-HGRMKEKEARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFTF--GN 204
Cdd:cd05073   89 KGSLLDFLKSdEGSKQPLPKLIDFSaQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLArviedNEYTAreGA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 205 KLDTfcgspPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDCENLLKK 283
Cdd:cd05073  169 KFPI-----KWTAPEAINFGSFT-IKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALERG-YRMP--RPENCPEELYN 239
                        250
                 ....*....|....*..
gi 564332436 284 FLI----LNPSKRGTLE 296
Cdd:cd05073  240 IMMrcwkNRPEERPTFE 256
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
53-356 1.18e-19

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: 91.28  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI-----ETEKTLYL 127
Cdd:cd07858    7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMppphrEAFNDVYI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGgEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN-EFTFGNKL 206
Cdd:cd07858   87 VYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARtTSEKGDFM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG----QNLKELRE---------------------- 260
Cdd:cd07858  166 TEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGkdyvHQLKLITEllgspseedlgfirnekarryi 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 261 RVLRGKYRIPF-----YMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLP-DYKDPRRTELMVs 334
Cdd:cd07858  246 RSLPYTPRQSFarlfpHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQTPFSfDFEEDALTEEDI- 324
                        330       340
                 ....*....|....*....|..
gi 564332436 335 mgytREEIqdslvgqrYNEVMA 356
Cdd:cd07858  325 ----KELI--------YNEMLA 334
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
52-312 1.41e-19

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: 90.93  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKE--VAVKIIDKTQLNSSSLQKLFREVRIMKVL-NHPNIVKLF--EVIETEK--T 124
Cdd:cd07857    1 RYELIKELGQGAYGIVCSARNAETSEEetVAIKKITNVFSKKILAKRALRELKLLRHFrGHKNITCLYdmDIVFPGNfnE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEyasggeVFDY-LVAHGRMKEKEARAKFR----QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE 199
Cdd:cd07857   81 LYLYEE------LMEAdLHQIIRSGQPLTDAHFQsfiyQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFG-----NKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKE----------------L 258
Cdd:cd07857  155 FSENpgenaGFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDqlnqilqvlgtpdeetL 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 259 RE----------RVLRGKYRIPF-----YMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHE-DDE 312
Cdd:cd07857  235 SRigspkaqnyiRSLPNIPKKPFesifpNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDpDDE 304
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
54-265 1.62e-19

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: 89.72  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLK---TIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIET----EKTLY 126
Cdd:cd14030   25 RFLKfdiEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF--IVHRDLKAENLLLDADM-NIKIADFGFSNeFTFG 203
Cdd:cd14030  105 LVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLAT-LKRA 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 204 NKLDTFCGSPPYAAPELFQgKKYDgPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRG 265
Cdd:cd14030  184 SFAKSVIGTPEFMAPEMYE-EKYD-ESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRRVTSG 244
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
59-266 1.73e-19

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: 89.23  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKE--VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEkTLYLVMEYASGGE 136
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQidVAIKVL-KQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAE-ALMLVMEMASGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHGRMKEKEARAKFRQIVS-AVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGN---KLDTFCGS 212
Cdd:cd05115   90 LNKFLSGKKDEITVSNVVELMHQVSmGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDsyyKARSAGKW 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 213 P-PYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGK 266
Cdd:cd05115  170 PlKWYAPECINFRKFSS-RSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFIEQGK 224
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
52-317 1.85e-19

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: 90.19  E-value: 1.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06615    2 DFEKLGELGAGNGGVVTKVLHRPSGLIMARKLI-HLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEF--TFGNkldT 208
Cdd:cd06615   81 MDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLidSMAN---S 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 209 FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKEL----------------RERVLRGKYRIPFY 272
Cdd:cd06615  158 FVGTRSYMSPERLQGTHY-TVQSDIWSLGLSLVEMAIGRYPIPPPDAKELeamfgrpvsegeakesHRPVSGHPPDSPRP 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 273 M----------------------STDCENLLKKFLILNPSKRGTLEQIMKDRW-MNVGHEDDELKPYV 317
Cdd:cd06615  237 MaifelldyivnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFiKRAELEEVDFAGWV 304
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
54-247 1.86e-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: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTI---GKGNFAKVKLARHIL----TGKEVAVKiidKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIET--EK 123
Cdd:cd05081    4 RHLKYIsqlGKGNFGSVELCRYDPlgdnTGALVAVK---QLQHSGPDQQRDFqREIQILKALHSDFIVKYRGVSYGpgRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:cd05081   81 SLRLVMEYLPSGCLRDFLQRHrARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564332436 203 GNKLDTF--CGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVSGS 247
Cdd:cd05081  161 DKDYYVVrePGQSPifWYAPESLSDNIFS-RQSDVWSFGVVLYELFTYC 208
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
62-298 1.91e-19

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: 89.10  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  62 GNFAKVKLARHILTGkEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYL 141
Cdd:cd14027    4 GGFGKVSLCFHRTQG-LVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 142 VAHGRMKEKEARAKFrQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN----------EFTFGNKLDTFC- 210
Cdd:cd14027   83 KKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskltkeEHNEQREVDGTAk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 211 ---GSPPYAAPELFQGKKYDGPE-VDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRGKY----RIPFYMSTDCENLL 281
Cdd:cd14027  162 knaGTLYYMAPEHLNDVNAKPTEkSDVYSFAIVLWAIFANKEPYeNAINEDQIIMCIKSGNRpdvdDITEYCPREIIDLM 241
                        250
                 ....*....|....*..
gi 564332436 282 KKFLILNPSKRGTLEQI 298
Cdd:cd14027  242 KLCWEANPEARPTFPGI 258
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
53-265 2.03e-19

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: 89.59  E-value: 2.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHIL---TGKEVAVKIIdKTQLNSSS-LQKLFREVRIMKVLNHPNIVKLFEVIETEKTL--- 125
Cdd:cd05074   11 FTLGRMLGKGEFGSVREAQLKSedgSFQKVAVKML-KADIFSSSdIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKgrl 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 ---YLVMEYASGGEVFDYLVAhGRMKEK------EARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG 195
Cdd:cd05074   90 pipMVILPFMKHGDLHTFLLM-SRIGEEpftlplQTLVRFMiDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFG 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 196 FSNEFTFGNKLDTFCGSP---PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG 265
Cdd:cd05074  169 LSKKIYSGDYYRQGCASKlpvKWLALESLADNVYT-THSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLIKG 241
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
59-299 2.62e-19

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: 88.94  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFR-EVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd05047    3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAgELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYL-------------VAHGRMKEKEARAKFR---QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-NE 199
Cdd:cd05047   83 LLDFLrksrvletdpafaIANSTASTLSSQQLLHfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSrGQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFGNKLdtfCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPFYMSTD 276
Cdd:cd05047  163 EVYVKKT---MGRLPvrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRLEKPLNCD 237
                        250       260
                 ....*....|....*....|....*
gi 564332436 277 CE--NLLKKFLILNPSKRGTLEQIM 299
Cdd:cd05047  238 DEvyDLMRQCWREKPYERPSFAQIL 262
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
54-243 2.75e-19

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: 89.32  E-value: 2.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLAR----HILTGKE------------VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFE 117
Cdd:cd05051    8 EFVEKLGEGQFGEVHLCEanglSDLTSDDfigndnkdepvlVAVKML-RPDASKNAREDFLKEVKIMSQLKDPNIVRLLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 118 VIETEKTLYLVMEYASGGEVFDYLVAHgRMKEKEARAKFR-------------QIVSAVQYCHQKFIVHRDLKAENLLLD 184
Cdd:cd05051   87 VCTRDEPLCMIVEYMENGDLNQFLQKH-EAETQGASATNSktlsygtllymatQIASGMKYLESLNFVHRDLATRNCLVG 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 185 ADMNIKIADFGFSNEFTFGN--KLDtfcGSPP----YAAPELFQGKKYDgPEVDVWSLGVIL---YTL 243
Cdd:cd05051  166 PNYTIKIADFGMSRNLYSGDyyRIE---GRAVlpirWMAWESILLGKFT-TKSDVWAFGVTLweiLTL 229
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
52-258 3.76e-19

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: 89.34  E-value: 3.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06650    6 DFEKISELGAGNGGVVFKVSHKPSGLVMARKLI-HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEFtFGNKLDTFC 210
Cdd:cd06650   85 MDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-IDSMANSFV 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKEL 258
Cdd:cd06650  164 GTRSYMSPERLQGTHYS-VQSDIWSMGLSLVEMAVGRYPIPPPDAKEL 210
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
53-267 4.51e-19

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: 89.20  E-value: 4.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTG-KEVAVKIIDktqlNSSSLQKL-FREVRIMKVLNH--PN----IVKLFEVIETEKT 124
Cdd:cd14135    2 YRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIR----NNELMHKAgLKELEILKKLNDadPDdkkhCIRLLRHFEHKNH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASggevfdylvahgrMKEKEARAKF-RQI---VSAVQ-YCHQKF----------IVHRDLKAENLLLDADMN- 188
Cdd:cd14135   78 LCLVFESLS-------------MNLREVLKKYgKNVglnIKAVRsYAQQLFlalkhlkkcnILHADIKPDNILVNEKKNt 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 189 IKIADFGfSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQN----LKELRErvLR 264
Cdd:cd14135  145 LKLCDFG-SASDIGENEITPYLVSRFYRAPEIILGLPYDYP-IDMWSVGCTLYELYTGKILFPGKTnnhmLKLMMD--LK 220

                 ...
gi 564332436 265 GKY 267
Cdd:cd14135  221 GKF 223
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
55-300 4.85e-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: 87.79  E-value: 4.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLAR-HiltgKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd14063    4 IKEVIGKGRFGRVHRGRwH----GDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLvaHGRmKEKEARAKFR----QIVSAVQYCHQKFIVHRDLKAENLLLDADmNIKIADFGFSN--EFTFGNKLD 207
Cdd:cd14063   80 GRTLYSLI--HER-KEKFDFNKTVqiaqQICQGMGYLHAKGIIHKDLKSKNIFLENG-RVVITDFGLFSlsGLLQPGRRE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSP----PYAAPEL---------FQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMS 274
Cdd:cd14063  156 DTLVIPngwlCYLAPEIiralspdldFEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQSLSQLD 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 275 TDCEnlLKKFLIL----NPSKRGTLEQIMK 300
Cdd:cd14063  236 IGRE--VKDILMQcwayDPEKRPTFSDLLR 263
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
59-245 5.69e-19

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: 87.53  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIidkTQLNSSSLQKLfREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVf 138
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSSNRANML-REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMN---IKIADFGFSNE---FTFGNKLDTFCG 211
Cdd:cd14155   76 EQLLDSNEPLSWTVRVKLAlDIARGLSYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLAEKipdYSDGKEKLAVVG 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564332436 212 SPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS 245
Cdd:cd14155  156 SPYWMAPEVLRGEPYN-EKADVFSYGIILCEIIA 188
UBA_MARK_Par1 cd14337
UBA domain found in microtubule-associated protein (MAP)/microtubule affinity-regulating ...
324-363 6.46e-19

UBA domain found in microtubule-associated protein (MAP)/microtubule affinity-regulating kinase (MARK)/ partitioning-defective 1 (Par-1) and similar proteins; The MARK/Par-1 subfamily contains serine/threonine-protein kinases including mammal MARKs, and polarity kinases Par-1 found in Caenorhabditis elegans and Drosophila melanogaster. Those proteins are frequently found associated with membrane structures and participate in diverse processes from control of the cell cycle and polarity to intracellular signaling and microtubule stability. They are involved in nematode embryogenesis, cell cycle control, epithelial cell polarization, cell signaling, and neuronal migration and differentiation. The mammals MARKs have been implicated in carcinomas, Alzheimer's disease (through tau hyperphosphorylation), and autism. Four MARK isoforms exist in humans. Members in this subfamily contain an N-terminal protein kinase catalytic domain, followed by an ubiquitin-associated (UBA) domain and a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK).


Pssm-ID: 270522  Cd Length: 40  Bit Score: 80.64  E-value: 6.46e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564332436 324 KDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY 363
Cdd:cd14337    1 PDPKRIEIMVSMGFNREEIEESLKNRKFDEVMATYLLLGR 40
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
54-250 9.52e-19

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: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKEVAVKII--DKTqlnsSSLQK-LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd06619    4 QYQEILGHGNGGTVYKAYHLLTRRILAVKVIplDIT----VELQKqIMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEvfdyLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKL-DTF 209
Cdd:cd06619   80 FMDGGS----LDVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--NSIaKTY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564332436 210 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd06619  154 VGTNAYMAPERISGEQY-GIHSDVWSLGISFMELALGRFPY 193
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
54-270 1.08e-18

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: 87.05  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTgKEVAVKIIDKTQLnssSLQKLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEYAS 133
Cdd:cd05071   12 RLEVKLGQGCFGEVWMGTWNGT-TRVAIKTLKPGTM---SPEAFLQEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVA-HGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-----NEFTF--GN 204
Cdd:cd05071   87 KGSLLDFLKGeMGKYLRLPQLVDMaAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLArliedNEYTArqGA 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 205 KLDTFCGSPPYAAPELFQGKKydgpevDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIP 270
Cdd:cd05071  167 KFPIKWTAPEAALYGRFTIKS------DVWSFGILLTELTTkGRVPYPGMVNREVLDQVERG-YRMP 226
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
57-286 1.17e-18

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: 86.95  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTG-KEVAVKIID-KTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASG 134
Cdd:cd05063   11 KVIGAGEFGEVFRGILKMPGrKEVAVAIKTlKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN------EFTFgnklD 207
Cdd:cd05063   91 GALDKYLRDHdGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRvleddpEGTY----T 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPP--YAAPELFQGKKYDGPEvDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPFYMstDCENLLKKF 284
Cdd:cd05063  167 TSGGKIPirWTAPEAIAYRKFTSAS-DVWSFGIVMWEVMSfGERPYWDMSNHEVMKAINDG-FRLPAPM--DCPSAVYQL 242

                 ..
gi 564332436 285 LI 286
Cdd:cd05063  243 ML 244
KA1 pfam02149
Kinase associated domain 1;
799-841 1.38e-18

Kinase associated domain 1;


Pssm-ID: 460465  Cd Length: 44  Bit Score: 79.82  E-value: 1.38e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564332436  799 VQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL 841
Cdd:pfam02149   2 VKFEIEVCKLPRLSLYGVDFKRLSGDTWQYKDLASKILSELRL 44
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
53-284 1.48e-18

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: 87.62  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSlQKLfrEVRIMKVLNH------PNIVKLFEVIETEKTLY 126
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREA-AKI--EIDVLETLAEkdpngkSHCVQLRDWFDYRGHMC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVME-YasGGEVFDYLVAHG----RMKEKEARAKfrQIVSAVQYCHQKFIVHRDLKAENLLLD----------------- 184
Cdd:cd14134   91 IVFElL--GPSLYDFLKKNNygpfPLEHVQHIAK--QLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrqir 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 185 --ADMNIKIADFG---FSNEFTfgnklDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDG-QNLKEL 258
Cdd:cd14134  167 vpKSTDIKLIDFGsatFDDEYH-----SSIVSTRHYRAPEVILGLGWSYP-CDVWSIGCILVELYTGELLFQThDNLEHL 240
                        250       260
                 ....*....|....*....|....*...
gi 564332436 259 R--ERVLrGKyrIPFYMSTDCENLLKKF 284
Cdd:cd14134  241 AmmERIL-GP--LPKRMIRRAKKGAKYF 265
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
59-260 2.33e-18

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: 85.65  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDktqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYK----NDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLVahgrmkEKEARAKFRQ-------IVSAVQYCHQKFIVHRDLKAENLLLDADMNIK---IADFGFSNEF-----TFG 203
Cdd:cd14156   77 ELLA------REELPLSWREkvelacdISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempaNDP 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 204 NKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVsGSLPFDGQNLKELRE 260
Cdd:cd14156  151 ERKLSLVGSAFWMAPEMLRGEPYD-RKVDVFSFGIVLCEIL-ARIPADPEVLPRTGD 205
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
76-298 2.37e-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: 85.94  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  76 GKEVAVKIIDKTQLNsssLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRmKEKEARAK 155
Cdd:cd05052   31 NLTVAVKTLKEDTME---VEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNR-EELNAVVL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 156 FR---QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFgnklDTFCGSP------PYAAPELFQGKKY 226
Cdd:cd05052  107 LYmatQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTG----DTYTAHAgakfpiKWTAPESLAYNKF 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 227 DgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRI--PFYMSTDCENLLKKFLILNPSKRGTLEQI 298
Cdd:cd05052  183 S-IKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKG-YRMerPEGCPPKVYELMRACWQWNPSDRPSFAEI 255
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
51-252 2.79e-18

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: 86.04  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARH--ILTGKE---VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL 125
Cdd:cd05050    5 NNIEYVRDIGQGAFGRVFQARApgLLPYEPftmVAVKML-KEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYL----------VAHGRMK------------EKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLL 183
Cdd:cd05050   84 CLLFEYMAYGDLNEFLrhrspraqcsLSHSTSSarkcglnplplsCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLV 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 184 DADMNIKIADFGFSNEFTFGN--KLDTFCGSP-PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDG 252
Cdd:cd05050  164 GENMVVKIADFGLSRNIYSADyyKASENDAIPiRWMPPESIFYNRYT-TESDVWAYGVVLWEIFSyGMQPYYG 235
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
45-251 2.84e-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: 86.01  E-value: 2.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  45 DEQPHIGNYRLLktiGKGNFAKVKLARhiLTGKEVAVK-IIDKTQLNSSSLQKLF-REVRIMKVLNHPNIVKLFEVIETE 122
Cdd:cd14158   12 DERPISVGGNKL---GEGGFGVVFKGY--INDKNVAVKkLAAMVDISTEDLTKQFeQEIQVMAKCQHENLVELLGYSCDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVMEYASGGEVFDYL---------VAHGRMKEKEARAKfrqivsAVQYCHQKFIVHRDLKAENLLLDADMNIKIAD 193
Cdd:cd14158   87 PQLCLVYTYMPNGSLLDRLaclndtpplSWHMRCKIAQGTAN------GINYLHENNHIHRDIKSANILLDETFVPKISD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332436 194 FGF---SNEFTFGNKLDTFCGSPPYAAPELFQGKKydGPEVDVWSLGVILYTLVSGSLPFD 251
Cdd:cd14158  161 FGLaraSEKFSQTIMTERIVGTTAYMAPEALRGEI--TPKSDIFSFGVVLLEIITGLPPVD 219
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
54-277 3.46e-18

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 85.83  E-value: 3.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK---LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05090    8 RFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQwneFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAH-------------GRMKEKEARAKFR----QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIAD 193
Cdd:cd05090   88 FMNQGDLHEFLIMRsphsdvgcssdedGTVKSSLDHGDFLhiaiQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 194 FGFSNEFTfgnKLDTFCGSPP------YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVlRGK 266
Cdd:cd05090  168 LGLSREIY---SSDYYRVQNKsllpirWMPPEAIMYGKFSS-DSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV-RKR 242
                        250
                 ....*....|.
gi 564332436 267 YRIPfyMSTDC 277
Cdd:cd05090  243 QLLP--CSEDC 251
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
54-265 4.10e-18

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: 85.13  E-value: 4.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLK---TIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIET----EKTLY 126
Cdd:cd14032    1 RFLKfdiELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWEScakgKRCIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF--IVHRDLKAENLLLDADM-NIKIADFGFSNeFTFG 203
Cdd:cd14032   81 LVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLAT-LKRA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 204 NKLDTFCGSPPYAAPELFQgKKYDgPEVDVWSLGVILYTLVSGSLPF-DGQNLKELRERVLRG 265
Cdd:cd14032  160 SFAKSVIGTPEFMAPEMYE-EHYD-ESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTCG 220
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
59-270 4.72e-18

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: 85.57  E-value: 4.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARhiLTGKEVAVKIIDktqlnSSSLQKLFREVRIMKV--LNHPNIVKLF----EVIETEKTLYLVMEYA 132
Cdd:cd13998    3 IGKGRFGEVWKAS--LKNEPVAVKIFS-----SRDKQSWFREKEIYRTpmLKHENILQFIaadeRDTALRTELWLVTAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAHG-------RMKEKEARA---KFRQIVSAVQycHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF 202
Cdd:cd13998   76 PNGSL*DYLSLHTidwvslcRLALSVARGlahLHSEIPGCTQ--GKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 203 G-NKLDTF----CGSPPYAAPELFQG----KKYDG-PEVDVWSLGVILYTLVS------GS-----LPFDGQ-----NLK 256
Cdd:cd13998  154 StGEEDNAnngqVGTKRYMAPEVLEGainlRDFESfKRVDIYAMGLVLWEMASrctdlfGIveeykPPFYSEvpnhpSFE 233
                        250
                 ....*....|....*.
gi 564332436 257 ELRERVLRGKYR--IP 270
Cdd:cd13998  234 DMQEVVVRDKQRpnIP 249
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
56-300 4.96e-18

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 85.21  E-value: 4.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLAR---HILTGKE--VAVKIIDKTQLNSSsLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05046   10 ITTLGRGEFGEVFLAKakgIEEEGGEtlVLVKALQKTKDENL-QSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAhGRMKEKEARAKFRQIVSAVQYCHQ----------KFIVHRDLKAENLLLDADMNIKIADFGFSNE- 199
Cdd:cd05046   89 YTDLGDLKQFLRA-TKSKDEKLKPPPLSTKQKVALCTQialgmdhlsnARFVHRDLAARNCLVSSQREVKVSLLSLSKDv 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 -----FTFGNKLdtfcgsPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKYRIPf 271
Cdd:cd05046  168 ynseyYKLRNAL------IPlrWLAPEAVQEDDFS-TKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELP- 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 272 yMSTDCENLLKKFL----ILNPSKRGTLEQIMK 300
Cdd:cd05046  240 -VPEGCPSRLYKLMtrcwAVNPKDRPSFSELVS 271
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
53-292 5.72e-18

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: 85.69  E-value: 5.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKiidKTQLNSSSLQKL-FREVRIMKVLN--HPNIVKL-------------- 115
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPENVELaLREFWALSSIQrqHPNVIQLeecvlqrdglaqrm 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 116 ----------FEVIET----EKT--------LYLVMEYASGGEVFDYLVAhgRMKEKEARAKF-RQIVSAVQYCHQKFIV 172
Cdd:cd13977   79 shgssksdlyLLLVETslkgERCfdprsacyLWFVMEFCDGGDMNEYLLS--RRPDRQTNTSFmLQLSSALAFLHRNQIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 173 HRDLKAENLLLDADMN---IKIADFGFS----------NEFTFGNK--LDTFCGSPPYAAPELFQGkkYDGPEVDVWSLG 237
Cdd:cd13977  157 HRDLKPDNILISHKRGepiLKVADFGLSkvcsgsglnpEEPANVNKhfLSSACGSDFYMAPEVWEG--HYTAKADIFALG 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 238 VILYTLVSGSLPFDGQNLKELR-ERVLRGKYRIPF--------------------YMSTDCENLLKKFLILNPSKR 292
Cdd:cd13977  235 IIIWAMVERITFRDGETKKELLgTYIQQGKEIVPLgeallenpklelqiplkkkkSMNDDMKQLLRDMLAANPQER 310
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
55-250 8.40e-18

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: 84.70  E-value: 8.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKlarhilTGK---EVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVkLFEVIETEKTLYLVMEY 131
Cdd:cd14149   16 LSTRIGSGSFGTVY------KGKwhgDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQW 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN---EFTFGNKLD 207
Cdd:cd14149   89 CEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVE 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564332436 208 TFCGSPPYAAPELFQGKKyDGP---EVDVWSLGVILYTLVSGSLPF 250
Cdd:cd14149  169 QPTGSILWMAPEVIRMQD-NNPfsfQSDVYSYGIVLYELMTGELPY 213
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
53-240 1.44e-17

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: 83.93  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTG-KEVAVKIIDKTQLNSSSLQKLFREVRIMKVLN---HPNIVKLFEVIETEKT---- 124
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDLKNGgRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVSRTdret 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 -LYLVMEYASGgEVFDYL--VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFT 201
Cdd:cd07862   83 kLTLVFEHVDQ-DLTTYLdkVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564332436 202 FGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVIL 240
Cdd:cd07862  162 FQMALTSVVVTLWYRAPEVLLQSSYATP-VDLWSVGCIF 199
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
59-317 1.62e-17

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: 83.90  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFR-EVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd05089   10 IGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAgELEVLcKLGHHPNIINLLGACENRGYLYIAIEYAPYGN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYL-------------VAHGRMKEKEARAKFR---QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS-NE 199
Cdd:cd05089   90 LLDFLrksrvletdpafaKEHGTASTLTSQQLLQfasDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLSrGE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFGNKLdtfCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPFYMSTD 276
Cdd:cd05089  170 EVYVKKT---MGRLPvrWMAIESLNYSVYT-TKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRMEKPRNCD 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564332436 277 CE--NLLKKFLILNPSKRGTLEQIMkdrwMNVGHEDDELKPYV 317
Cdd:cd05089  245 DEvyELMRQCWRDRPYERPPFSQIS----VQLSRMLEARKAYV 283
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
55-250 1.66e-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: 84.27  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNF--AKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd08216    2 LLYEIGKCFKggGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAH---GrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIAdfGFSNEFTF---GNKL 206
Cdd:cd08216   82 AYGSCRDLLKTHfpeG-LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLS--GLRYAYSMvkhGKRQ 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 207 DTFCGSP-------PYAAPEL----FQGkkYDgPEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd08216  159 RVVHDFPksseknlPWLSPEVlqqnLLG--YN-EKSDIYSVGITACELANGVVPF 210
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
57-303 2.03e-17

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: 83.48  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARhiLTGKEVAVKIidktqLNSSSLQKLFREVRI--MKVLNHPNIVKLF------EVIETEktLYLV 128
Cdd:cd14056    1 KTIGKGRYGEVWLGK--YRGEKVAVKI-----FSSRDEDSWFRETEIyqTVMLRHENILGFIaadiksTGSWTQ--LWLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHgRMKEKEARAKFRQIVSAVQYCHQKF--------IVHRDLKAENLLLDADMNIKIADFGFSneF 200
Cdd:cd14056   72 TEYHEHGSLYDYLQRN-TLDTEEALRLAYSAASGLAHLHTEIvgtqgkpaIAHRDLKSKNILVKRDGTCCIADLGLA--V 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 TFGNKLDTF-------CGSPPYAAPEL----FQGKKYDG-PEVDVWSLGVILY-----TLVSG-----SLPFDGQ----- 253
Cdd:cd14056  149 RYDSDTNTIdippnprVGTKRYMAPEVlddsINPKSFESfKMADIYSFGLVLWeiarrCEIGGiaeeyQLPYFGMvpsdp 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564332436 254 NLKELRERVLRGKYRIPFymstdcENLLKKFLILNPskrgtLEQIMKDRW 303
Cdd:cd14056  229 SFEEMRKVVCVEKLRPPI------PNRWKSDPVLRS-----MVKLMQECW 267
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
53-254 2.07e-17

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: 84.57  E-value: 2.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------Y 126
Cdd:cd07879   17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGdefqdfY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGevFDYLVAHgRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgNKL 206
Cdd:cd07879   97 LVMPYMQTD--LQKIMGH-PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHAD--AEM 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 207 DTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd07879  172 TGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKD 219
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
54-298 4.32e-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: 82.28  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKE---VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd05064    8 KIERILGTGRFGELCRGCLKLPSKRelpVAIHTL-RAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 YASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTF 209
Cdd:cd05064   87 YMSNGALDSFLRKHeGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQEDKSEAIYTTM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 210 CGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDCENLLKKFLI 286
Cdd:cd05064  167 SGKSPvlWAAPEAIQYHHFS-SASDVWSFGIVMWEVMSyGERPYWDMSGQDVIKAVEDG-FRLP--APRNCPNLLHQLML 242
                        250
                 ....*....|....*.
gi 564332436 287 ----LNPSKRGTLEQI 298
Cdd:cd05064  243 dcwqKERGERPRFSQI 258
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
59-251 4.53e-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: 82.16  E-value: 4.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARhILTGKEVAVKIIDKTQLNSSSLQkLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 138
Cdd:cd14664    1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 DYLvaHGRMKEKEA---RAKFRQIVSAVQ---YCHQK---FIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK--LD 207
Cdd:cd14664   79 ELL--HSRPESQPPldwETRQRIALGSARglaYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDShvMS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564332436 208 TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFD 251
Cdd:cd14664  157 SVAGSYGYIAPEYAYTGKVS-EKSDVYSYGVVLLELITGKRPFD 199
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
52-258 4.58e-17

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: 83.17  E-value: 4.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEY 131
Cdd:cd06649    6 DFERISELGAGNGGVVTKVQHKPSGLIMARKLI-HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEFtFGNKLDTFC 210
Cdd:cd06649   85 MDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-IDSMANSFV 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564332436 211 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKEL 258
Cdd:cd06649  164 GTRSYMSPERLQGTHYS-VQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
57-315 5.86e-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: 81.84  E-value: 5.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHILTGKE---VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05065   10 EVIGAGEFGEVCRGRLKLPGKReifVAIKTL-KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGS 212
Cdd:cd05065   89 NGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 213 -----P-PYAAPELFQGKKYDGPEvDVWSLGVILYTLVS-GSLPF-DGQNLKELreRVLRGKYRIPFYMstDCenllkkf 284
Cdd:cd05065  169 lggkiPiRWTAPEAIAYRKFTSAS-DVWSYGIVMWEVMSyGERPYwDMSNQDVI--NAIEQDYRLPPPM--DC------- 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564332436 285 lilnPSkrgTLEQIMKDRWMnvghEDDELKP 315
Cdd:cd05065  237 ----PT---ALHQLMLDCWQ----KDRNLRP 256
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-254 6.83e-17

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: 82.75  E-value: 6.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKII--DKTQLNSSSLqklfrEVRIMKVLNHP------NIVKLFEVIETEKT 124
Cdd:cd14226   15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIknKKAFLNQAQI-----EVRLLELMNKHdtenkyYIVRLKRHFMFRNH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 125 LYLVMEYASgGEVFDYLvahgrmKEKEARA-------KF-RQIVSAVQYCHQK--FIVHRDLKAENLLLdadMN-----I 189
Cdd:cd14226   90 LCLVFELLS-YNLYDLL------RNTNFRGvslnltrKFaQQLCTALLFLSTPelSIIHCDLKPENILL---CNpkrsaI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 190 KIADFGFSNefTFGNKLDTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQN 254
Cdd:cd14226  160 KIIDFGSSC--QLGQRIYQYIQSRFYRSPEVLLGLPYDLA-IDMWSLGCILVEMHTGEPLFSGAN 221
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
100-246 8.74e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 83.51  E-value: 8.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 100 EVRIMKVLNHPNIVKLFEVIETEKTLYLVM-EYASggEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKA 178
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLILpRYKT--DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKA 210
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332436 179 ENLLLDADMNIKIADFG---FSNEFTfGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSG 246
Cdd:PHA03212 211 ENIFINHPGDVCLGDFGaacFPVDIN-ANKYYGWAGTIATNAPELLARDPY-GPAVDIWSAGIVLFEMATC 279
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
55-301 9.27e-17

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: 81.59  E-value: 9.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVKLARhiLTGKE----VAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI--ETEKTLY-- 126
Cdd:cd05075    4 LGKTLGEGEFGSVMEGQ--LNQDDsvlkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVClqNTESEGYps 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 --LVMEYASGGEVFDYLVaHGRMKEK------EARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS 197
Cdd:cd05075   82 pvVILPFMKHGDLHSFLL-YSRLGDCpvylptQMLVKFmTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 NEFTFGN--KLDTFCGSP-PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG-KYRIPfy 272
Cdd:cd05075  161 KKIYNGDyyRQGRISKMPvKWIAIESLADRVYT-TKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQGnRLKQP-- 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564332436 273 msTDCENLLKKFLI----LNPSKRGTLEQIMKD 301
Cdd:cd05075  238 --PDCLDGLYELMSscwlLNPKDRPSFETLRCE 268
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
75-300 1.92e-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: 80.83  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  75 TGKEVAVKIIDKTQLNSSS-------LQKLFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVME--YASGGEVF------ 138
Cdd:cd14011   20 TKQEVSVFVFEKKQLEEYSkrdreqiLELLKRGVKQLTRLRHPRILTVQHPLEESReSLAFATEpvFASLANVLgerdnm 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 139 ----DYLVAHGrMKEKEARAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDADMNIKIADFGFSNEFT-FGNKLDTFCG- 211
Cdd:cd14011  100 psppPELQDYK-LYDVEIKYGLLQISEALSFLHNDVkLVHGNICPESVVINSNGEWKLAGFDFCISSEqATDQFPYFREy 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 212 ----------SPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDG--------QNLKELRERVLRGKYRIPFy 272
Cdd:cd14011  179 dpnlpplaqpNLNYLAPEYILSKTCD-PASDMFSLGVLIYAIYNkGKPLFDCvnnllsykKNSNQLRQLSLSLLEKVPE- 256
                        250       260
                 ....*....|....*....|....*...
gi 564332436 273 MSTDCenlLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14011  257 ELRDH---VKTLLNVTPEVRPDAEQLSK 281
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
55-300 1.96e-16

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: 80.78  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKV--KLARHILTGkEVAVKIIDKTQLNSSSLQK---LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVM 129
Cdd:cd05061   10 LLRELGQGSFGMVyeGNARDIIKG-EAETRVAVKTVNESASLRErieFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVA--------HGRMKE--KEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE 199
Cdd:cd05061   89 ELMAHGDLKSYLRSlrpeaennPGRPPPtlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 ------FTFGNKldtfcGSPP--YAAPELFQgkkyDG---PEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKY 267
Cdd:cd05061  169 iyetdyYRKGGK-----GLLPvrWMAPESLK----DGvftTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDGGY 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564332436 268 ripFYMSTDCE----NLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd05061  240 ---LDQPDNCPervtDLMRMCWQFNPKMRPTFLEIVN 273
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
15-264 2.43e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 82.82  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  15 DTEQPTLGHLDSKPSSKSNMLRGRNSATSADEqpHIGNYRLLKTIGKGNFAKVKL-ARHILTGKEVAVKIIDKTQLNSSS 93
Cdd:PHA03210 114 DSDASHLDFDEAPPDAAGPVPLAQAKLKHDDE--FLAHFRVIDDLPAGAFGKIFIcALRASTEEAEARRGVNSTNQGKPK 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  94 LQKLF---------------REVRIMKVLNHPNIVKLFEVIETEKTLYLVME-YASGGEVFDY---LVAHGRMKEKEARA 154
Cdd:PHA03210 192 CERLIakrvkagsraaiqleNEILALGRLNHENILKIEEILRSEANTYMITQkYDFDLYSFMYdeaFDWKDRPLLKQTRA 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 155 KFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG----FSNE---FTFGnkldtFCGSPPYAAPELFQGKKYd 227
Cdd:PHA03210 272 IMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGtampFEKEreaFDYG-----WVGTVATNSPEILAGDGY- 345
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564332436 228 gPEV-DVWSLGVILYTLVSGSLPFDGQNLKELRERVLR 264
Cdd:PHA03210 346 -CEItDIWSCGLILLDMLSHDFCPIGDGGGKPGKQLLK 382
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
57-268 2.88e-16

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: 80.06  E-value: 2.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARhiLTGKEVAVKIIDKTQLNS-SSLQKLFREVRimkvLNHPNIV------KLFEVIETEktLYLVM 129
Cdd:cd14053    1 EIKARGRFGAVWKAQ--YLNRLVAVKIFPLQEKQSwLTEREIYSLPG----MKHENILqfigaeKHGESLEAE--YWLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHgRMKEKEARAKFRQIVSAVQYCH----------QKFIVHRDLKAENLLLDADMNIKIADFGFSNE 199
Cdd:cd14053   73 EFHERGSLCDYLKGN-VISWNELCKIAESMARGLAYLHedipatngghKPSIAHRDFKSKNVLLKSDLTACIADFGLALK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFGNKL-DTF--CGSPPYAAPELFQGKKYDGPE----VDVWSLGVILYTLVSGS-----------LPFD---GQ--NLK 256
Cdd:cd14053  152 FEPGKSCgDTHgqVGTRRYMAPEVLEGAINFTRDaflrIDMYAMGLVLWELLSRCsvhdgpvdeyqLPFEeevGQhpTLE 231
                        250
                 ....*....|..
gi 564332436 257 ELRERVLRGKYR 268
Cdd:cd14053  232 DMQECVVHKKLR 243
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
61-301 3.29e-16

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: 79.74  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  61 KGNFAKVKLARHILTGKE-------VAVKIIDKtqlNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd13992    3 CGSGASSHTGEPKYVKKVgvyggrtVAIKHITF---SRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLvahgRMKEKEARAKFR-----QIVSAVQYCHQKFI-VHRDLKAENLLLDADMNIKIADFGFSNeFTFGNKLD 207
Cdd:cd13992   80 RGSLQDVL----LNREIKMDWMFKssfikDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRN-LLEEQTNH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPP-----YAAPELFQGKKYDG---PEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRG--KYRIP--FYMST 275
Cdd:cd13992  155 QLDEDAQhkkllWTAPELLRGSLLEVrgtQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGgnKPFRPelAVLLD 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 564332436 276 DCEN----LLKKFLILNPSKRGTLEQIMKD 301
Cdd:cd13992  235 EFPPrlvlLVKQCWAENPEKRPSFKQIKKT 264
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
59-250 6.60e-16

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: 78.71  E-value: 6.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKiidKTQLnssslqKLFR--EVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVK---KVRL------EVFRaeELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD-MNIKIADFGFSNEFT---FGNKL---DTF 209
Cdd:cd13991   85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLDpdgLGKSLftgDYI 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564332436 210 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPF 250
Cdd:cd13991  165 PGTETHMAPEVVLGKPCDA-KVDVWSSCCMMLHMLNGCHPW 204
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
52-265 7.27e-16

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 78.58  E-value: 7.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHI-LTGKEVAVKIIDKTQLNSSSLQK---LFREVRIMKVLNHPNIVKLFEVIETEKTLYL 127
Cdd:cd05036    7 NLTLIRALGQGAFGEVYEGTVSgMPGDPSPLQVAVKTLPELCSEQDemdFLMEALIMSKFNHPNIVRCIGVCFQRLPRFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 128 VMEYASGGEVFDYLVAHGRMKEKEARAKF-------RQIVSAVQYCHQKFIVHRDLKAENLLL---DADMNIKIADFGFS 197
Cdd:cd05036   87 LLELMAGGDLKSFLRENRPRPEQPSSLTMldllqlaQDVAKGCRYLEENHFIHRDIAARNCLLtckGPGRVAKIGDFGMA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 198 NEF---TFGNKLDTFCGSPPYAAPELFQgkkyDG---PEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG 265
Cdd:cd05036  167 RDIyraDYYRKGGKAMLPVKWMPPEAFL----DGiftSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFVTSG 237
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
54-262 8.47e-16

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 78.52  E-value: 8.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTG-----KEVAVKII-DKTQLnssSLQKLFREVRIMKV-LNHPNIVKLFEVIETEKTLY 126
Cdd:cd05091    9 RFMEELGEDRFGKVYKGHLFGTApgeqtQAVAIKTLkDKAEG---PLREEFRHEAMLRSrLQHPNIVCLLGVVTKEQPMS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 127 LVMEYASGGEVFDYLVAHG------------RMKEKEARAKF----RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05091   86 MIFSYCSHGDLHEFLVMRSphsdvgstdddkTVKSTLEPADFlhivTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVK 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 191 IADFGFSNEFTFGNKLDTFCGSP---PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERV 262
Cdd:cd05091  166 ISDLGLFREVYAADYYKLMGNSLlpiRWMSPEAIMYGKFS-IDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMI 240
UBA_MARK3_4 cd14407
UBA domain found in MAP/microtubule affinity-regulating kinase MARK3, MARK4, and similar ...
322-364 1.03e-15

UBA domain found in MAP/microtubule affinity-regulating kinase MARK3, MARK4, and similar proteins; MARK3, also called C-TAK1, Cdc25C-associated protein kinase 1, ELKL motif kinase 2 (EMK-2), protein kinase STK10, Ser/Thr protein kinase PAR-1 (Par-1a), or serine/threonine-protein kinase p78, is a known regulator of KSR1, a molecular scaffold of the Raf/MEK/ERK MAP kinase cascade that regulates the intensity and duration of ERK activation. It binds plakophilin 2 (PKP2), phosphorylates human Cdc25C on serine 216, and promotes 14-3-3 protein binding and protein localization. It also interacts with microphthalmia-associated transcription factor, Mitf which is necessary for regulating genes involved in osteoclast differentiation. Moreover, MARK3 is involved in regulating localization and activity of class IIa histone deacetylases. The lack of MARK3 leads to reduced adiposity, resistance to hepatic steatosis, and defective gluconeogenesis. MARK4, also called MAP/microtubule affinity-regulating kinase-like 1 (MARKL1), or Par-1d, is a member of the AMP-activated protein kinase (AMPK)-related family of kinases. It plays a key role in energy metabolism and may act as a novel drug target for the treatment of obesity and type 2 diabetes. MARK4 also functions as the substrate of ubiquitin specific protease-9 (USP9X) and can be regulated by unusual Lys(29)/Lys(33)-linked polyubiquitin chains. Furthermore, MARK4 may play some role in hepatocellular carcinogenesis.


Pssm-ID: 270590  Cd Length: 43  Bit Score: 71.44  E-value: 1.03e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564332436 322 DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYK 364
Cdd:cd14407    1 DISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRK 43
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
59-250 2.16e-15

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: 77.31  E-value: 2.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLAR--HILTGKE---VAVKIIdkTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYAS 133
Cdd:cd05092   13 LGEGAFGKVFLAEchNLLPEQDkmlVAVKAL--KEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVAH---------------GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSN 198
Cdd:cd05092   91 HGDLNRFLRSHgpdakildggegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSR 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564332436 199 EFtFGNKLDTFCGSP----PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPF 250
Cdd:cd05092  171 DI-YSTDYYRVGGRTmlpiRWMPPESILYRKFT-TESDIWSFGVVLWEIFTyGKQPW 225
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
59-317 2.84e-15

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: 77.35  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFR-EVRIM-KVLNHPNIVKLFEVIETEKTLYLVMEYASGGE 136
Cdd:cd05088   15 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAgELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 137 VFDYL-------------VAH---GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNef 200
Cdd:cd05088   95 LLDFLrksrvletdpafaIANstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 201 tfGNK--LDTFCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPFYMST 275
Cdd:cd05088  173 --GQEvyVKKTMGRLPvrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQG-YRLEKPLNC 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564332436 276 DCE--NLLKKFLILNPSKRGTLEQIMkdrwMNVGHEDDELKPYV 317
Cdd:cd05088  249 DDEvyDLMRQCWREKPYERPSFAQIL----VSLNRMLEERKTYV 288
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
53-254 3.77e-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: 77.68  E-value: 3.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIdKTQLnsSSLQKLFREVRIMKVLN-------HPNIVKLFEVIETEKTL 125
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKP--AYFRQAMLEIAILTLLNtkydpedKHHIVRLLDHFMHHGHL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYAsGGEVFDYLVA---HGrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADM--NIKIADFG---FS 197
Cdd:cd14212   78 CIVFELL-GVNLYELLKQnqfRG-LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIKLIDFGsacFE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 198 NEFTFgnkldTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGsLP-FDGQN 254
Cdd:cd14212  156 NYTLY-----TYIQSRFYRSPEVLLGLPYSTA-IDMWSLGCIAAELFLG-LPlFPGNS 206
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
55-275 4.41e-15

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 77.22  E-value: 4.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKG--NFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV---M 129
Cdd:cd08226    2 LQVELGKGfcNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVIspfM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAHGrMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIAdfGFSNEFTF---GNKL 206
Cdd:cd08226   82 AYGSARGLLKTYFPEG-MNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLS--GLSHLYSMvtnGQRS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 207 DTFCGSP-------PYAAPELFQGKKYdGPEV--DVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMST 275
Cdd:cd08226  159 KVVYDFPqfstsvlPWLSPELLRQDLH-GYNVksDIYSVGITACELARGQVPFQDMRRTQMLLQKLKGPPYSPLDIFP 235
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
59-303 4.67e-15

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: 77.03  E-value: 4.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHI--LTGKEVAVKIIDKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVI--ETEKTLYLVMEYASG 134
Cdd:cd07867   10 VGRGTYGHVYKAKRKdgKDEKEYALKQIEGTGISMSAC----REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 gEVFDYLVAHGRMKEKE---------ARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD----MNIKIADFGFSNEFT 201
Cdd:cd07867   86 -DLWHIIKFHRASKANKkpmqlprsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNK----LDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSG-------------SLPF-------------- 250
Cdd:cd07867  165 SPLKpladLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSepifhcrqediktSNPFhhdqldrifsvmgf 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332436 251 ----DGQNLKELRER-VLRGKYRIPFYMSTDCEN---------------LLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07867  245 padkDWEDIRKMPEYpTLQKDFRRTTYANSSLIKymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 317
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
100-260 6.17e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 78.01  E-value: 6.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 100 EVRIMKVLNHPNIVKLFEVIETEKTLYLVM-EYASggEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKFIVHRDLK 177
Cdd:PHA03211 210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLpKYRS--DLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGIIHRDIK 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 178 AENLLLDADMNIKIADFG--------FSNEFTFGnkldtFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILY-------T 242
Cdd:PHA03211 288 TENVLVNGPEDICLGDFGaacfargsWSTPFHYG-----IAGTVDTNAPEVLAGDPYT-PSVDIWSAGLVIFeaavhtaS 361
                        170       180
                 ....*....|....*....|...
gi 564332436 243 LVSGSL-----PFDGQNLKELRE 260
Cdd:PHA03211 362 LFSASRgderrPYDAQILRIIRQ 384
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
159-292 6.20e-15

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty 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: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 75.60  E-value: 6.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 159 IVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNklDTFCGSPPYAAPELFQGkKYDGpEVDVWSLGV 238
Cdd:cd13975  111 VVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMS--GSIVGTPIHMAPELFSG-KYDN-SVDVYAFGI 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332436 239 ILYTLVSGS--LPFDGQNLK---ELRERVLRGKY--RIPFYmSTDCENLLKKFLILNPSKR 292
Cdd:cd13975  187 LFWYLCAGHvkLPEAFEQCAskdHLWNNVRKGVRpeRLPVF-DEECWNLMEACWSGDPSQR 246
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
44-245 8.99e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.84  E-value: 8.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  44 ADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKtqlnSSSLQklfrEVRIMKVLNHPNIVKLFEVIETEK 123
Cdd:PHA03209  59 AREVVASLGYTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQK----GTTLI----EAMLLQNVNHPSVIRMKDTLVSGA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 124 TLYLVMEYASGgEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGfSNEFTF 202
Cdd:PHA03209 131 ITCMVLPHYSS-DLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPV 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564332436 203 GNKLDT-FCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVS 245
Cdd:PHA03209 209 VAPAFLgLAGTVETNAPEVLARDKYNS-KADIWSAGIVLFEMLA 251
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
55-265 1.42e-14

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: 74.88  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKV---KLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTL------ 125
Cdd:cd05035    3 LGKILGEGEFGSVmeaQLKQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppsp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 126 YLVMEYASGGEVFDYLVAH--GRMKEK---EARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNE 199
Cdd:cd05035   83 MVILPFMKHGDLHSYLLYSrlGGLPEKlplQTLLKFMvDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRK 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 200 FTFGNKLDTFCGSP---PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRG 265
Cdd:cd05035  163 IYSGDYYRQGRISKmpvKWIALESLADNVYT-SKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNG 231
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
51-304 2.01e-14

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: 75.31  E-value: 2.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  51 GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQ---KLFREVRIM--KVLNHPNIVKL---FEVI-ET 121
Cdd:cd14136   10 GRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALdeiKLLKCVREAdpKDPGREHVVQLlddFKHTgPN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 122 EKTLYLVMEYasGGE-------VFDY------LVahgrmkekeaRAKFRQIVSAVQYCHQKF-IVHRDLKAENLLLDA-D 186
Cdd:cd14136   90 GTHVCMVFEV--LGPnllklikRYNYrgiplpLV----------KKIARQVLQGLDYLHTKCgIIHTDIKPENVLLCIsK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 187 MNIKIADFG----FSNEFTfgNKLDTfcgsPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQ--------- 253
Cdd:cd14136  158 IEVKIADLGnacwTDKHFT--EDIQT----RQYRSPEVILGAGYGTP-ADIWSTACMAFELATGDYLFDPHsgedysrde 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 254 -----------------------------------NLKELR----ERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGT 294
Cdd:cd14136  231 dhlaliiellgriprsiilsgkysreffnrkgelrHISKLKpwplEDVLVEKYKWSKEEAKEFASFLLPMLEYDPEKRAT 310
                        330
                 ....*....|
gi 564332436 295 LEQIMKDRWM 304
Cdd:cd14136  311 AAQCLQHPWL 320
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
57-300 2.55e-14

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: 74.21  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARHilTGKEVAVK--IIDKTQLNSSSLQKLFREVRiMKVLNHPNIVKLFEVIETEKTLYLVMEYAsG 134
Cdd:cd13980    6 KSLGSTRFLKVARARH--DEGLVVVKvfVKPDPALPLRSYKQRLEEIR-DRLLELPNVLPFQKVIETDKAAYLIRQYV-K 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADF-GF-------SNEFTFGNKL 206
Cdd:cd13980   82 YNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFaSFkptylpeDNPADFSYFF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DT----FCgsppYAAPELFQGK-KYDG----------PEVDVWSLG-VILYTLVSGSLPFDGQNLKELRervlRGKYRIP 270
Cdd:cd13980  162 DTsrrrTC----YIAPERFVDAlTLDAeserrdgeltPAMDIFSLGcVIAELFTEGRPLFDLSQLLAYR----KGEFSPE 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564332436 271 FYMS----TDCENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd13980  234 QVLEkiedPNIRELILHMIQRDPSKRLSAEDYLK 267
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
59-303 2.82e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 75.09  E-value: 2.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHI--LTGKEVAVKIIDKTQLNSSSLqklfREVRIMKVLNHPNIVKLFEVI--ETEKTLYLVMEYASG 134
Cdd:cd07868   25 VGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGISMSAC----REIALLRELKHPNVISLQKVFlsHADRKVWLLFDYAEH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 gEVFDYLVAHGRMKEKE---------ARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDAD----MNIKIADFGFSNEFT 201
Cdd:cd07868  101 -DLWHIIKFHRASKANKkpvqlprgmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 202 FGNK----LDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSG-------------SLPF-------------- 250
Cdd:cd07868  180 SPLKpladLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSepifhcrqediktSNPYhhdqldrifnvmgf 259
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 251 ----DGQNLKELRER-VLRGKYRIPFYmsTDCE-----------------NLLKKFLILNPSKRGTLEQIMKDRW 303
Cdd:cd07868  260 padkDWEDIKKMPEHsTLMKDFRRNTY--TNCSlikymekhkvkpdskafHLLQKLLTMDPIKRITSEQAMQDPY 332
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
53-292 2.84e-14

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: 74.67  E-value: 2.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  53 YRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSL---QKLFREVRIMKVLNHPNIVKLFEVIETEkTLYLVM 129
Cdd:cd05108    9 FKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPkanKEILDEAYVMASVDNPHVCRLLGICLTS-TVQLIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK-LD 207
Cdd:cd05108   88 QLMPFGCLLDYVREHkDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKeYH 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKyRIPF--YMSTDCENLLK 282
Cdd:cd05108  168 AEGGKVPikWMALESILHRIYTH-QSDVWSYGVTVWELMTfGSKPYDGIPASEISSILEKGE-RLPQppICTIDVYMIMV 245
                        250
                 ....*....|
gi 564332436 283 KFLILNPSKR 292
Cdd:cd05108  246 KCWMIDADSR 255
UBA_MARK1 cd14405
UBA domain found in serine/threonine-protein kinase MARK1 and similar proteins; MARK1, also ...
325-364 3.15e-14

UBA domain found in serine/threonine-protein kinase MARK1 and similar proteins; MARK1, also called MAP/microtubule affinity-regulating kinase 1 or PAR1 homolog c (Par-1c), is a kinase-regulating microtubule-dependent transport in axons and dendrites. It is involved in the specification of neuronal polarity, in axon-dendrite specification, and in the synaptic plasticity in adult neurons. It has been implicated in Alzheimer's disease, cancer, and autism.


Pssm-ID: 270588  Cd Length: 41  Bit Score: 67.24  E-value: 3.15e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564332436 325 DPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYK 364
Cdd:cd14405    2 DTKRIDIMVTMGFSRDEINEALVNQKYDEVMATYLLLGRK 41
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-204 3.43e-14

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: 74.24  E-value: 3.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKL--ARHIL----------TGKE--VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVI 119
Cdd:cd05097    8 RLKEKLGEGQFGEVHLceAEGLAeflgegapefDGQPvlVAVKML-RADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 120 ETEKTLYLVMEYASGGEVFDYLvahgrmKEKEARAKFR------------------QIVSAVQYCHQKFIVHRDLKAENL 181
Cdd:cd05097   87 VSDDPLCMITEYMENGDLNQFL------SQREIESTFThannipsvsianllymavQIASGMKYLASLNFVHRDLATRNC 160
                        170       180
                 ....*....|....*....|...
gi 564332436 182 LLDADMNIKIADFGFSNEFTFGN 204
Cdd:cd05097  161 LVGNHYTIKIADFGMSRNLYSGD 183
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
56-270 8.16e-14

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: 73.18  E-value: 8.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARHILTGKEV----AVKIIDKTQLNSSSLQkLFREVRIMKVLNHPNIVKLFEVIeTEKTLYLVMEY 131
Cdd:cd05110   12 VKVLGSGAFGTVYKGIWVPEGETVkipvAIKILNETTGPKANVE-FMDEALIMASMDHPHLVRLLGVC-LSPTIQLVTQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNK-LDTF 209
Cdd:cd05110   90 MPHGCLLDYVHEHKDNIGSQLLLNWcVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKeYNAD 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332436 210 CGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKyRIP 270
Cdd:cd05110  170 GGKMPikWMALECIHYRKFTH-QSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLLEKGE-RLP 231
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
54-270 1.10e-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: 72.30  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  54 RLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKlFREVR----IMKVLNHPNIVKLFEVIETeKTLYLVM 129
Cdd:cd05111   10 RKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQS-FQAVTdhmlAIGSLDHAYIVRLLGICPG-ASLQLVT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 130 EYASGGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFS------NEFTF 202
Cdd:cd05111   88 QLLPLGSLLDHVRQHrGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVAdllypdDKKYF 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332436 203 GNKLDTfcgSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKyRIP 270
Cdd:cd05111  168 YSEAKT---PIKWMALESIHFGKYTH-QSDVWSYGVTVWEMMTfGAEPYAGMRLAEVPDLLEKGE-RLA 231
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
52-283 1.50e-13

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 71.52  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQlnssSLQKLFREVRIMKVL-NHPNIVKLFEVIETEKTLYLVME 130
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQ----PKQVLKMEVAVLKKLqGKPHFCRLIGCGRTERYNYIVMT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 131 yasggevfdyLVAH--GRMKEKEARAKF---------RQIVSAVQYCHQKFIVHRDLKAENLLL---DADM-NIKIADFG 195
Cdd:cd14017   77 ----------LLGPnlAELRRSQPRGKFsvsttlrlgIQILKAIEDIHEVGFLHRDVKPSNFAIgrgPSDErTVYILDFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 196 FSNEFTFGNKLDT--------FCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgQNLKElRERVLRGKY 267
Cdd:cd14017  147 LARQYTNKDGEVErpprnaagFRGTVRYASVNAHRNKEQ-GRRDDLWSWFYMLIEFVTGQLPW--RKLKD-KEEVGKMKE 222
                        250
                 ....*....|....*.
gi 564332436 268 RIpfymstDCENLLKK 283
Cdd:cd14017  223 KI------DHEELLKG 232
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-304 1.72e-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: 72.81  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  49 HIG-NYRLLKTIGKGNFAKVKLARHILTGKEVAVKII-DKTQLNSSSLQklfrEVRIMKVL------NHPNIVKLFEVIE 120
Cdd:cd14225   40 HIAyRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIrNKKRFHHQALV----EVKILDALrrkdrdNSHNVIHMKEYFY 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 121 TEKTLYLVMEYASggevfdyLVAHGRMKEKEAR----AKFRQIVSAVQYC----HQKFIVHRDLKAENLLLD--ADMNIK 190
Cdd:cd14225  116 FRNHLCITFELLG-------MNLYELIKKNNFQgfslSLIRRFAISLLQClrllYRERIIHCDLKPENILLRqrGQSSIK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 191 IADFGfSNEFTFgNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQN---------------- 254
Cdd:cd14225  189 VIDFG-SSCYEH-QRVYTYIQSRFYRSPEVILGLPY-SMAIDMWSLGCILAELYTGYPLFPGENeveqlacimevlglpp 265
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332436 255 ---LKELRERVL--------------RGKYRIP----FYMSTDCE-----NLLKKFLILNPSKRGTLEQIMKDRWM 304
Cdd:cd14225  266 pelIENAQRRRLffdskgnprcitnsKGKKRRPnskdLASALKTSdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
52-266 2.00e-13

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: 71.61  E-value: 2.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  52 NYRLLKTIGKGNFAKVKLAR-HILTGKEVAVKIIDKT--QLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLV 128
Cdd:cd05093    6 NIVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTlkDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHG-------------RMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG 195
Cdd:cd05093   86 FEYMKHGDLNKFLRAHGpdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332436 196 FSNEF--TFGNKLDTFCGSP-PYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGK 266
Cdd:cd05093  166 MSRDVysTDYYRVGGHTMLPiRWMPPESIMYRKFT-TESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGR 239
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
55-293 2.45e-13

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 71.90  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKG--NFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYA 132
Cdd:cd08227    2 LLTVIGRGfeDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 133 SGGEVFDYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIAdfGFSNEFTF---GNKLD 207
Cdd:cd08227   82 AYGSAKDLICTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMinhGQRLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSP-------PYAAPELFQG--KKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKyrIPFYMstDCE 278
Cdd:cd08227  160 VVHDFPkysvkvlPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGT--VPCLL--DTT 234
                        250
                 ....*....|....*
gi 564332436 279 NLLKKFLILNPSKRG 293
Cdd:cd08227  235 TIPAEELTMKPSRSG 249
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
57-306 2.67e-13

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 71.08  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  57 KTIGKGNFAKVKLARhILTGKEVAVKIIDKTQLNSSSLQ--KLFREVRIMKVLNHPNIVK-LFEVIETEKTLyLVMEYAS 133
Cdd:cd05042    1 QEIGNGWFGKVLLGE-IYSGTSVAQVVVKELKASANPKEqdTFLKEGQPYRILQHPNILQcLGQCVEAIPYL-LVMEFCD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 134 GGEVFDYLVA---HGRMkEKEARAKFR---QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSneftFGNKLD 207
Cdd:cd05042   79 LGDLKAYLRSereHERG-DSDTRTLQRmacEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLA----HSRYKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 208 TFCGSPP-------YAAPEL---FQGKKY---DGPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKY-RIPfy 272
Cdd:cd05042  154 DYIETDDklwfplrWTAPELvteFHDRLLvvdQTKYSNIWSLGVTLWELFEnGAQPYSNLSDLDVLAQVVREQDtKLP-- 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564332436 273 mstdcenllkkflilnpskRGTLEQIMKDRWMNV 306
Cdd:cd05042  232 -------------------KPQLELPYSDRWYEV 246
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
80-249 2.74e-13

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 71.28  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  80 AVKIID-KTQLNSSSL--QKLFREVRIMKVLNHPNIVKLFEVIETEK-TLYLVMEYAsGGEVFDYLVAhgRMKEKE---- 151
Cdd:cd14001   32 AVKKINsKCDKGQRSLyqERLKEEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYG-GKSLNDLIEE--RYEAGLgpfp 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 152 ARAKFR---QIVSAVQYCHQ-KFIVHRDLKAENLLLDADMN-IKIADFGFS-----NEFTFGNKLDTFCGSPPYAAPELF 221
Cdd:cd14001  109 AATILKvalSIARALEYLHNeKKILHGDIKSGNVLIKGDFEsVKLCDFGVSlplteNLEVDSDPKAQYVGTEPWKAKEAL 188
                        170       180       190
                 ....*....|....*....|....*....|.
gi 564332436 222 QGkkyDGP---EVDVWSLGVILYTLVSGSLP 249
Cdd:cd14001  189 EE---GGVitdKADIFAYGLVLWEMMTLSVP 216
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
59-204 2.80e-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: 71.56  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLAR----HILTGKE------------VAVKIIdKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETE 122
Cdd:cd05095   13 LGEGQFGEVHLCEaegmEKFMDKDfalevsenqpvlVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 123 KTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFR------------QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIK 190
Cdd:cd05095   92 DPLCMITEYMENGDLNQFLSRQQPEGQLALPSNALtvsysdlrfmaaQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 171
                        170
                 ....*....|....
gi 564332436 191 IADFGFSNEFTFGN 204
Cdd:cd05095  172 IADFGMSRNLYSGD 185
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
55-300 2.90e-13

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 71.32  E-value: 2.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  55 LLKTIGKGNFAKVklARHILTGKEVAVKIidktqLNSSSLQKLFREVRIMK--VLNHPNIVKLFEVIETEKT----LYLV 128
Cdd:cd14142    9 LVECIGKGRYGEV--WRGQWQGESVAVKI-----FSSRDEKSWFRETEIYNtvLLRHENILGFIASDMTSRNsctqLWLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 129 MEYASGGEVFDYLVAHgrmkEKEARAKFRQIVSAVQ---------YCHQ--KFIVHRDLKAENLLLDADMNIKIADFGFS 197
Cdd:cd14142   82 THYHENGSLYDYLQRT----TLDHQEMLRLALSAASglvhlhteiFGTQgkPAIAHRDLKSKNILVKSNGQCCIADLGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 198 NEFTFG-NKLDTFC----GSPPYAAPEL---------FQGKKydgpEVDVWSLGVILY-----TLVSG-----------S 247
Cdd:cd14142  158 VTHSQEtNQLDVGNnprvGTKRYMAPEVldetintdcFESYK----RVDIYAFGLVLWevarrCVSGGiveeykppfydV 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 248 LPFDgQNLKELRERVLRGKYR--IPFYMSTD-----CENLLKKFLILNPSKRGTLEQIMK 300
Cdd:cd14142  234 VPSD-PSFEDMRKVVCVDQQRpnIPNRWSSDptltaMAKLMKECWYQNPSARLTALRIKK 292
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
110-292 3.64e-13

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: 70.65  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 110 PNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKE-----------ARAKFR-----------QIVSAVQYCH 167
Cdd:cd05576   51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKFLNDKEIHqlfadlderlaAASRFYipeeciqrwaaEMVVALDALH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 168 QKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTfgnklDTFCG---SPPYAAPELfQGKKYDGPEVDVWSLGVILYTLV 244
Cdd:cd05576  131 REGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVE-----DSCDSdaiENMYCAPEV-GGISEETEACDWWSLGALLFELL 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564332436 245 SGslpfdgqnlKELRERVLRG-----KYRIPFYMSTDCENLLKKFLILNPSKR 292
Cdd:cd05576  205 TG---------KALVECHPAGinthtTLNIPEWVSEEARSLLQQLLQFNPTER 248
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
59-270 5.17e-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: 69.81  E-value: 5.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  59 IGKGNFAKVKLARHILTGKE---VAVKIIDKTQlNSSSLQKLFREVRIMKVLNHPNIVKLFEV-IETEKTLYLVMEYASG 134
Cdd:cd05058    3 IGKGHFGCVYHGTLIDSDGQkihCAVKSLNRIT-DIEEVEQFLKEGIIMKDFSHPNVLSLLGIcLPSEGSPLVVLPYMKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 135 GEVFDYLVAHGRMKEKEARAKF-RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFG-----FSNEF-----TFG 203
Cdd:cd05058   82 GDLRNFIRSETHNPTVKDLIGFgLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGlardiYDKEYysvhnHTG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332436 204 NKLDTfcgspPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGKyRIP 270
Cdd:cd05058  162 AKLPV-----KWMALESLQTQKFT-TKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLQGR-RLL 222
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
88-265 6.23e-13

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 69.99  E-value: 6.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  88 QLNSSSLQKLFREVR----IMKVLNHPNIVKLFEV----------IETEKTLYLVMEYASGGEVFdylVAHGRM-KEKEA 152
Cdd:cd14067   44 HLRAADAMKNFSEFRqeasMLHSLQHPCIVYLIGIsihplcfaleLAPLGSLNTVLEENHKGSSF---MPLGHMlTFKIA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 153 RakfrQIVSAVQYCHQKFIVHRDLKAENLL---LDAD--MNIKIADFGFSNEfTFGNKLDTFCGSPPYAAPELFQGKKYD 227
Cdd:cd14067  121 Y----QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQehINIKLSDYGISRQ-SFHEGALGVEGTPGYQAPEIRPRIVYD 195
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564332436 228 gPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRG 265
Cdd:cd14067  196 -EKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
56-298 1.00e-12

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 69.25  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436  56 LKTIGKGNFAKVKLARhILTGKEVAvKIIDKTQLNSSSLQ---KLFREVRIMKVLNHPNIVKLFEVIeTEKTLYL-VMEY 131
Cdd:cd05087    2 LKEIGHGWFGKVFLGE-VNSGLSST-QVVVKELKASASVQdqmQFLEEAQPYRALQHTNLLQCLAQC-AEVTPYLlVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 132 ASGGEVFDYL----VAHGRMKEKEARAKFR-QIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNeftFGNKL 206
Cdd:cd05087   79 CPLGDLKGYLrscrAAESMAPDPLTLQRMAcEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSH---CKYKE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332436 207 DTFCGSPP------YAAPELFQGKKYDGPEVD------VWSLGVILYTLVS-GSLPFDGQNLKE-----LRERVLR-GKY 267
Cdd:cd05087  156 DYFVTADQlwvplrWIAPELVDEVHGNLLVVDqtkqsnVWSLGVTIWELFElGNQPYRHYSDRQvltytVREQQLKlPKP 235
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564332436 268 RIPFYMSTDCENLLkKFLILNPSKRGTLEQI 298
Cdd:cd05087  236 QLKLSLAERWYEVM-QFCWLQPEQRPTAEEV 265
 
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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