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Conserved domains on  [gi|332078559|ref|NP_001193658|]
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RAC-gamma serine/threonine-protein kinase isoform 2 [Homo sapiens]

Protein Classification

PKB/RAC family serine/threonine-protein kinase( domain architecture ID 10100831)

PKB/RAC family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it contains an N-terminal pleckstrin homology (PH) domain and is activated downstream of phosphoinositide 3-kinase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
152-451 0e+00

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: 684.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPE 311
Cdd:cd05571   81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGG 391
Cdd:cd05571  161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 392 GPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05571  241 GPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDR 300
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-110 7.48e-76

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269947  Cd Length: 107  Bit Score: 232.52  E-value: 7.48e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   4 VTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVI 83
Cdd:cd01241    1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKPNQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTVI 80
                         90       100
                 ....*....|....*....|....*..
gi 332078559  84 ERTFHVDTPEEREEWTEAIQAVADRLQ 110
Cdd:cd01241   81 ERTFHVESEEEREEWMKAIQGVASSLK 107
 
Name Accession Description Interval E-value
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
152-451 0e+00

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: 684.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPE 311
Cdd:cd05571   81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGG 391
Cdd:cd05571  161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 392 GPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05571  241 GPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDR 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
148-405 2.11e-111

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 329.11  E-value: 2.11e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-KLFELILMEDIKFPR---TLSSDAKSLLSGLLIK 383
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLVK 237
                          250       260
                   ....*....|....*....|..
gi 332078559   384 DPNKRLGggpddAKEIMRHSFF 405
Cdd:smart00220 238 DPEKRLT-----AEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
133-436 1.12e-106

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 319.84  E-value: 1.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 133 MDASTTHHKRKT----MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFL 208
Cdd:PTZ00263   1 MKAAYMFTKPDTsswkLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 209 TSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 288
Cdd:PTZ00263  81 VNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEgITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT 368
Cdd:PTZ00263 161 DFGFAKK-VPDRTF--TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNW 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFD 436
Cdd:PTZ00263 238 FDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE 305
Pkinase pfam00069
Protein kinase domain;
148-405 1.86e-78

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 243.31  E-value: 1.86e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSgkivyrdlklenlmldkdghikitdfglckegitdaatMKTFC 307
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSS--------------------------------------LTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKD 384
Cdd:pfam00069 122 GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPElpsNLSEEAKDLLKKLLKKD 201
                         250       260
                  ....*....|....*....|.
gi 332078559  385 PNKRLGggpddAKEIMRHSFF 405
Cdd:pfam00069 202 PSKRLT-----ATQALQHPWF 217
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-110 7.48e-76

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269947  Cd Length: 107  Bit Score: 232.52  E-value: 7.48e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   4 VTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVI 83
Cdd:cd01241    1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKPNQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTVI 80
                         90       100
                 ....*....|....*....|....*..
gi 332078559  84 ERTFHVDTPEEREEWTEAIQAVADRLQ 110
Cdd:cd01241   81 ERTFHVESEEEREEWMKAIQGVASSLK 107
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
151-401 5.64e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 5.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK-TFCGT 309
Cdd:COG0515   92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTgTVVGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDA----KSLLSGLLIKDP 385
Cdd:COG0515  172 PGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLppalDAIVLRALAKDP 251
                        250
                 ....*....|....*.
gi 332078559 386 NKRlgggPDDAKEIMR 401
Cdd:COG0515  252 EER----YQSAAELAA 263
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
224-346 4.35e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 92.94  E-value: 4.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK----EGITD 299
Cdd:NF033483  85 VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARalssTTMTQ 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 300 AATMktfCGTPEYLAPEVLEdndyGRAV----DWWGLGVVMYEMMCGRLPF 346
Cdd:NF033483 165 TNSV---LGTVHYLSPEQAR----GGTVdarsDIYSLGIVLYEMLTGRPPF 208
PH pfam00169
PH domain; PH stands for pleckstrin homology.
6-105 3.98e-15

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 71.05  E-value: 3.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559    6 IVKEGWVQKRGEYIK-NWRPRYFLLKtDGSFIGYKEKPQDVDLPyPLNNFSVAKCQLMKTER----PKPNTFIIRCLQWT 80
Cdd:pfam00169   1 VVKEGWLLKKGGGKKkSWKKRYFVLF-DGSLLYYKDDKSGKSKE-PKGSISLSGCEVVEVVAsdspKRKFCFELRTGERT 78
                          90       100
                  ....*....|....*....|....*
gi 332078559   81 TVIERTFHVDTPEEREEWTEAIQAV 105
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
6-107 3.26e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 65.65  E-value: 3.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559     6 IVKEGWVQKRGE-YIKNWRPRYFLLkTDGSFIGYKEKPQDVDL----PYPLNNFSVAKCqLMKTERPKPNTFIIRCLQWT 80
Cdd:smart00233   1 VIKEGWLYKKSGgGKKSWKKRYFVL-FNSTLLYYKSKKDKKSYkpkgSIDLSGCTVREA-PDPDSSKKPHCFEIKTSDRK 78
                           90       100
                   ....*....|....*....|....*..
gi 332078559    81 TVIertFHVDTPEEREEWTEAIQAVAD 107
Cdd:smart00233  79 TLL---LQAESEEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
152-451 0e+00

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: 684.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPE 311
Cdd:cd05571   81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGG 391
Cdd:cd05571  161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 392 GPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05571  241 GPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDR 300
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
132-461 0e+00

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: 668.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 132 EMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSL 211
Cdd:cd05593    1 EMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 212 KYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd05593   81 KYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSS 371
Cdd:cd05593  161 LCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 372 DAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05593  241 DAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 320
                        330
                 ....*....|
gi 332078559 452 cqQSDCGMLG 461
Cdd:cd05593  321 --YDEDGMDC 328
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
152-456 0e+00

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: 646.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPE 311
Cdd:cd05595   81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGG 391
Cdd:cd05595  161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 392 GPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKCQQSD 456
Cdd:cd05595  241 GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLD 305
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
126-451 0e+00

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: 607.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 126 DNIGEEEMDASTTHHKRK-TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTR 204
Cdd:cd05594    4 DNSGAEEMEVSLTKPKHKvTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 205 HPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK-IVYRDLKLENLMLDKDG 283
Cdd:cd05594   84 HPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 284 HIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDI 363
Cdd:cd05594  164 HIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 364 KFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQT 443
Cdd:cd05594  244 RFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQM 323

                 ....*...
gi 332078559 444 ITITPPEK 451
Cdd:cd05594  324 ITITPPDQ 331
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
152-451 5.31e-166

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: 470.16  E-value: 5.31e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05570   81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05570  161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 391 GGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05570  241 CGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDS 301
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
152-456 4.18e-160

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: 455.62  E-value: 4.18e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05575   81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05575  161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 391 GGpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTItitPPEKCQQSD 456
Cdd:cd05575  241 SG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPV---PASVGKSAD 302
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
154-405 7.86e-153

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: 434.25  E-value: 7.86e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYL 313
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 314 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGP 393
Cdd:cd05123  161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSGG 240
                        250
                 ....*....|..
gi 332078559 394 ddAKEIMRHSFF 405
Cdd:cd05123  241 --AEEIKAHPFF 250
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
148-450 6.81e-140

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: 404.38  E-value: 6.81e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK---NTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRErVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd05589   81 MEYAAGGDLMMHIHED-VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd05589  160 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKN 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 385 PNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPE 450
Cdd:cd05589  240 PERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPK 305
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
152-451 2.65e-136

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: 394.83  E-value: 2.65e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK-NTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05592  161 DYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 391 GGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05592  241 VPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPVDK 301
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
151-450 4.56e-130

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: 379.06  E-value: 4.56e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKA---SGKYYAMKILKKEVII--AKDeVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05584    1 LKVLGKGGYGKVFQVRKTTgsdKGKIFAMKVLKKASIVrnQKD-TAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd05584   80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 385
Cdd:cd05584  160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 386 NKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPE 450
Cdd:cd05584  240 SSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVDSPDD 304
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
146-436 1.01e-129

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: 376.92  E-value: 1.01e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAAtmKT 305
Cdd:cd05580   81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR-VKDRT--YT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 385
Cdd:cd05580  158 LCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 386 NKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFD 436
Cdd:cd05580  238 TKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
151-456 6.68e-129

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: 376.23  E-value: 6.68e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd05604   81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd05604  161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 390 GGGpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTItitPPEKCQQSD 456
Cdd:cd05604  241 GAK-EDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMV---PYSVCVSSD 303
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
151-451 9.86e-129

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: 375.58  E-value: 9.86e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK-NTRHPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd05587   81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd05587  161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 390 GGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05587  241 GCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDK 302
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
152-456 1.54e-128

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: 375.46  E-value: 1.54e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05603   81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05603  161 EYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLG 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332078559 391 GGPdDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQ----TITITP---PEKCQQSD 456
Cdd:cd05603  241 AKA-DFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEavphSVGRTPdltASSSSSSS 312
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
152-448 3.37e-125

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: 366.82  E-value: 3.37e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK-NTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05591   81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05591  161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 391 --GGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITP 448
Cdd:cd05591  241 cvASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTP 300
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
146-444 4.24e-124

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: 364.72  E-value: 4.24e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd05602    7 SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd05602   87 LDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd05602  167 TFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKD 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 385 PNKRLgGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTI 444
Cdd:cd05602  247 RTKRL-GAKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPV 305
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
152-451 7.95e-124

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: 363.46  E-value: 7.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05590   81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05590  161 DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 391 GGPDDAKE-IMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05590  241 SLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEE 302
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
147-451 2.31e-119

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: 351.99  E-value: 2.31e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK-NTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 385
Cdd:cd05616  161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHP 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 386 NKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSEtDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05616  241 GKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRFFTRHPPVLTPPDQ 305
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
153-463 6.85e-112

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: 332.61  E-value: 6.85e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEY 312
Cdd:cd05585   81 LFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 313 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGG 392
Cdd:cd05585  161 LAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYN 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332078559 393 pdDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTI--TITPPEKCQQSDCGMLGNW 463
Cdd:cd05585  241 --GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPidSVVDDSHLSESVQQQFEGW 311
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
152-448 8.18e-112

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: 332.44  E-value: 8.18e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVRE---KASGKYYAMKILKKEVIIAKDEVaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05582    1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDRV-RTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG 308
Cdd:cd05582   80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 309 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd05582  160 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANR 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 389 LGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITP 448
Cdd:cd05582  240 LGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSP 299
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
154-440 1.25e-111

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: 332.61  E-value: 1.25e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNT---RHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR-TLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd05586  161 EYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 389 LgGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFT 440
Cdd:cd05586  241 L-GAHDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFT 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
148-405 2.11e-111

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 329.11  E-value: 2.11e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-KLFELILMEDIKFPR---TLSSDAKSLLSGLLIK 383
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLVK 237
                          250       260
                   ....*....|....*....|..
gi 332078559   384 DPNKRLGggpddAKEIMRHSFF 405
Cdd:smart00220 238 DPEKRLT-----AEEALQHPFF 254
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
152-448 3.79e-109

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: 325.91  E-value: 3.79e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETaSNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05588   81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--------YNQDHEK-LFELILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd05588  161 NYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDyLFQVILEKPIRIPRSLSVKAASVLKGFL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 382 IKDPNKRLGGGPDDA-KEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITP 448
Cdd:cd05588  241 NKNPAERLGCHPQTGfADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTP 308
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
145-451 9.38e-109

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: 325.41  E-value: 9.38e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLaLQDKPPFLTQLHSCFQTVDRLYF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd05615   89 VMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIK 383
Cdd:cd05615  169 RTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTK 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 384 DPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSEtDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05615  249 HPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFTRGQPVLTPPDQ 315
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
147-437 1.98e-108

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: 322.82  E-value: 1.98e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTDAATMkTF 306
Cdd:cd14209   82 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKR--VKGRTW-TL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPN 386
Cdd:cd14209  159 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLT 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 387 KRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDE 437
Cdd:cd14209  239 KRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
144-439 5.63e-108

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: 323.03  E-value: 5.63e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLC 222
Cdd:cd05619    3 TIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAT 302
Cdd:cd05619   83 FVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd05619  163 TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFV 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 383 KDPNKRLGGGPDdakeIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEF 439
Cdd:cd05619  243 REPERRLGVRGD----IRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEF 295
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
147-449 1.97e-107

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: 321.87  E-value: 1.97e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVReKASG----KYYAMKILKKEVIIAKDEVA-HTLTESRVLKNTRH-PFLTSLKYSFQTKDR 220
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVR-KVSGhdanKLYAMKVLRKAALVQKAKTVeHTRTERNVLEHVRQsPFLVTLHYAFQTDAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT-D 299
Cdd:cd05614   80 LHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTeE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY----NQDHEKLFELILMEDIKFPRTLSSDAK 374
Cdd:cd05614  160 KERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFPSFIGPVAR 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 375 SLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPP 449
Cdd:cd05614  240 DLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPA 314
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
133-436 1.12e-106

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 319.84  E-value: 1.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 133 MDASTTHHKRKT----MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFL 208
Cdd:PTZ00263   1 MKAAYMFTKPDTsswkLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 209 TSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 288
Cdd:PTZ00263  81 VNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEgITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT 368
Cdd:PTZ00263 161 DFGFAKK-VPDRTF--TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNW 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFD 436
Cdd:PTZ00263 238 FDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE 305
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
152-451 1.12e-103

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: 311.49  E-value: 1.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK-NTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLAlAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd05620   81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd05620  161 DYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 391 ggpdDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05620  241 ----VVGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSYSDK 297
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
147-436 1.58e-103

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: 310.52  E-value: 1.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMktf 306
Cdd:cd05612   82 YVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTL--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPN 386
Cdd:cd05612  159 CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRT 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 387 KRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFD 436
Cdd:cd05612  239 RRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFD 288
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
154-408 7.69e-102

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: 305.09  E-value: 7.69e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVRE---KASGKYYAMKILKKEVIIAKDEVA-HTLTESRVLKNTRH-PFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05583    2 LGTGAYGKVFLVRKvggHDAGKLYAMKVLKKATIVQKAKTAeHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA-ATMKTFC 307
Cdd:cd05583   82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGEnDRAYSFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFELILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd05583  162 GTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGernsQSEISKRILKSHPPIPKTFSAEAKDFILKLL 241
                        250       260
                 ....*....|....*....|....*..
gi 332078559 382 IKDPNKRLGGGPDDAKEIMRHSFFSGV 408
Cdd:cd05583  242 EKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
147-426 3.51e-101

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: 305.32  E-value: 3.51e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05574    2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK---------- 294
Cdd:cd05574   82 YCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtpppvr 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 --------------------EGITDAATMkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 354
Cdd:cd05574  162 kslrkgsrrssvksieketfVAEPSARSN-SFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDET 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 355 FELILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRLG--GGpddAKEIMRHSFFSGVNWQDVydKKLVPPFKPQV 426
Cdd:cd05574  241 FSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGskRG---ASEIKRHPFFRGVNWALI--RNMTPPIIPRP 311
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
145-451 5.06e-101

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: 306.56  E-value: 5.06e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQaSSNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF----YNQD---HEKLFELILMEDIKFPRTLSSDAKSL 376
Cdd:cd05617  174 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitDNPDmntEDYLFQVILEKPIRIPRFLSVKASHV 253
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 377 LSGLLIKDPNKRLGGGPDDA-KEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05617  254 LKGFLNKDPKERLGCQPQTGfSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDE 329
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
146-437 5.05e-100

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: 303.44  E-value: 5.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM-- 303
Cdd:cd05573   81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDREsy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 ---------------------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFE 356
Cdd:cd05573  161 lndsvntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 357 LIL--MEDIKFPR--TLSSDAKSLLSGLLIkDPNKRLGggpdDAKEIMRHSFFSGVNWQDVYDkkLVPPFKPQVTSETDT 432
Cdd:cd05573  241 KIMnwKESLVFPDdpDVSPEAIDLIRRLLC-DPEDRLG----SAEEIKAHPFFKGIDWENLRE--SPPPFVPELSSPTDT 313

                 ....*
gi 332078559 433 RYFDE 437
Cdd:cd05573  314 SNFDD 318
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
147-424 5.22e-100

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: 301.15  E-value: 5.22e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKA---SGKYYAMKILKKEVIIAKDEVA-HTLTESRVLKNTRH-PFLTSLKYSFQTKDRL 221
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKAKTAeHTRTERQVLEHIRQsPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 301
Cdd:cd05613   81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMK-TFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFY----NQDHEKLFELILMEDIKFPRTLSSDAK 374
Cdd:cd05613  161 ERAySFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALAK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 375 SLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05613  241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
145-451 1.77e-99

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: 302.72  E-value: 1.77e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05618   19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQaSNHPFLVGLHSCFQTESRLFF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd05618   99 VIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--------YNQDHEK-LFELILMEDIKFPRTLSSDAK 374
Cdd:cd05618  179 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDyLFQVILEKQIRIPRSLSVKAA 258
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 375 SLLSGLLIKDPNKRLGGGPDDA-KEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEK 451
Cdd:cd05618  259 SVLKSFLNKDPKERLGCHPQTGfADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDD 336
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
156-410 1.98e-95

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: 288.73  E-value: 1.98e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 156 KGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFF 235
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 236 HLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM------------ 303
Cdd:cd05579   83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKlsiqkksngape 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 ---KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR--TLSSDAKSLLS 378
Cdd:cd05579  163 kedRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKDLIS 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 379 GLLIKDPNKRLGGGPddAKEIMRHSFFSGVNW 410
Cdd:cd05579  243 KLLTPDPEKRLGAKG--IEEIKNHPFFKGIDW 272
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
146-450 5.84e-95

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: 289.51  E-value: 5.84e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKeGITDAATMKT 305
Cdd:cd05599   81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHLAYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLSGLL 381
Cdd:cd05599  160 TVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIERLL 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 382 IkDPNKRLGGGpdDAKEIMRHSFFSGVNWQDVYDKKlvPPFKPQVTSETDTRYFDEEFTAQTITITPPE 450
Cdd:cd05599  240 C-DAEHRLGAN--GVEEIKSHPFFKGVDWDHIRERP--APILPEVKSILDTSNFDEFEEVDLQIPSSPE 303
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
151-402 1.55e-92

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: 280.56  E-value: 1.55e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14003    5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTP 310
Cdd:cd14003   84 GELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-FRGGSLLKTFCGTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd14003  163 AYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRI 242
                        250
                 ....*....|...
gi 332078559 390 GggpddAKEIMRH 402
Cdd:cd14003  243 T-----IEEILNH 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
147-404 1.88e-90

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: 275.51  E-value: 1.88e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE-EMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgITDAATM 303
Cdd:cd05117   80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEGEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSG 379
Cdd:cd05117  159 KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLIKR 238
                        250       260
                 ....*....|....*....|....*
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd05117  239 LLVVDPKKRL-----TAAEALNHPW 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
147-404 2.83e-88

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 269.73  E-value: 2.83e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIaKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQ-KSGLEHQLRrEIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTDAATMKT 305
Cdd:cd14007   80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH--APSNRRKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 385
Cdd:cd14007  158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDP 237
                        250
                 ....*....|....*....
gi 332078559 386 NKRLgggpdDAKEIMRHSF 404
Cdd:cd14007  238 SKRL-----SLEQVLNHPW 251
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
154-412 9.28e-88

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: 268.71  E-value: 9.28e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYL 313
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTPEYV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 314 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE--KLFELILME--DIKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd05572  160 APEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPEERL 239
                        250       260
                 ....*....|....*....|...
gi 332078559 390 GGGPDDAKEIMRHSFFSGVNWQD 412
Cdd:cd05572  240 GYLKGGIRDIKKHKWFEGFDWEG 262
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
146-405 3.48e-87

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: 267.93  E-value: 3.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG----LCKEGITDAA 301
Cdd:cd05581   81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvLGPDSSPEST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMK-------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT 368
Cdd:cd05581  161 KGDadsqiaynqaraaSFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPEN 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLGGGPD-DAKEIMRHSFF 405
Cdd:cd05581  241 FPPDAKDLIQKLLVLDPSKRLGVNENgGYDELKAHPFF 278
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
148-405 9.23e-86

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: 263.35  E-value: 9.23e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd05578   82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK-LTDGTLATSTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd05578  161 GTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFetaSVLYPAGWSEEAIDLINKLLERD 240
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRLGggpdDAKEIMRHSFF 405
Cdd:cd05578  241 PQKRLG----DLSDLKNHPYF 257
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
146-437 3.31e-85

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: 264.56  E-value: 3.31e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG-LCKEGITDAATM 303
Cdd:cd05601   81 EYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGsAAKLSSDKTVTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLE--DND----YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFP--RTLSSDA 373
Cdd:cd05601  161 KMPVGTPDYIAPEVLTsmNGGskgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPedPKVSESA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 374 KSLLSGLLiKDPNKRLGGgpddaKEIMRHSFFSGVNWQDVYDKklVPPFKPQVTSETDTRYFDE 437
Cdd:cd05601  241 VDLIKGLL-TDAKERLGY-----EGLCCHPFFSGIDWNNLRQT--VPPFVPTLTSDDDTSNFDE 296
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
154-424 8.32e-82

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: 254.37  E-value: 8.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPE 311
Cdd:cd05577   81 KYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVGTHG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPN 386
Cdd:cd05577  160 YMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPE 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 387 KRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05577  240 RRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
146-436 7.04e-81

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: 253.78  E-value: 7.04e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05598    1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKeGITDAATMKT 305
Cdd:cd05598   81 DYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDSKY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FC-----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEDIKFPRT--LSSDAKSL 376
Cdd:cd05598  160 YLahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQtpAETQLKVINWRTTLKIPHEanLSPEAKDL 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 377 LSGlLIKDPNKRLGGGpdDAKEIMRHSFFSGVNWQdvYDKKLVPPFKPQVTSETDTRYFD 436
Cdd:cd05598  240 ILR-LCCDAEDRLGRN--GADEIKAHPFFAGIDWE--KLRKQKAPYIPTIRHPTDTSNFD 294
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
147-410 3.80e-80

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: 250.02  E-value: 3.80e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM--- 303
Cdd:cd05609   81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNlye 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 ------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR---T 368
Cdd:cd05609  161 ghiekdtrefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEgddA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLGGGpdDAKEIMRHSFFSGVNW 410
Cdd:cd05609  241 LPDDAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
141-437 4.90e-80

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: 253.42  E-value: 4.90e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 141 KRKT---MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQT 217
Cdd:cd05600    3 KRRTrlkLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 297
Cdd:cd05600   83 PENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDA--------------------------ATMKTF-----------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd05600  163 SPKkiesmkirleevkntafleltakerrNIYRAMrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 341 CGRLPFY---------NQDH-EKLFELILMEDIKFPRTLSSDAKSLLSgLLIKDPNKRLGGgpddAKEIMRHSFFSGVNW 410
Cdd:cd05600  243 VGFPPFSgstpnetwaNLYHwKKTLQRPVYTDPDLEFNLSDEAWDLIT-KLITDPQDRLQS----PEQIKNHPFFKNIDW 317
                        330       340
                 ....*....|....*....|....*..
gi 332078559 411 qDVYDKKLVPPFKPQVTSETDTRYFDE 437
Cdd:cd05600  318 -DRLREGSKPPFIPELESEIDTSYFDD 343
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
147-449 2.25e-79

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: 249.57  E-value: 2.25e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05597    2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC----KEGITDAA 301
Cdd:cd05597   82 YYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClklrEDGTVQSS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMktfCGTPEYLAPEVLEDND-----YGRAVDWWGLGVVMYEMMCGRLPFYNQ----------DHEKLFELILMEDikfp 366
Cdd:cd05597  162 VA---VGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAEslvetygkimNHKEHFSFPDDED---- 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 367 rTLSSDAKSLLSGlLIKDPNKRLG-GGPDDakeIMRHSFFSGVNWQDVYDkkLVPPFKPQVTSETDTRYFDEEFTAQTIT 445
Cdd:cd05597  235 -DVSEEAKDLIRR-LICSRERRLGqNGIDD---FKKHPFFEGIDWDNIRD--STPPYIPEVTSPTDTSNFDVDDDDLRHT 307

                 ....
gi 332078559 446 ITPP 449
Cdd:cd05597  308 DSLP 311
Pkinase pfam00069
Protein kinase domain;
148-405 1.86e-78

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 243.31  E-value: 1.86e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSgkivyrdlklenlmldkdghikitdfglckegitdaatMKTFC 307
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSS--------------------------------------LTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKD 384
Cdd:pfam00069 122 GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPElpsNLSEEAKDLLKKLLKKD 201
                         250       260
                  ....*....|....*....|.
gi 332078559  385 PNKRLGggpddAKEIMRHSFF 405
Cdd:pfam00069 202 PSKRLT-----ATQALQHPWF 217
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
148-424 1.34e-77

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: 243.42  E-value: 1.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd05605   82 MNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGETIRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd05605  161 RVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSICSQLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 332078559 382 IKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05605  241 QKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
142-437 1.10e-76

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: 243.44  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 142 RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd05596   22 RMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHLSRERvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC----KEGI 297
Cdd:cd05596  102 YMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmkmdKDGL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 --TDAATmktfcGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR-- 367
Cdd:cd05596  181 vrSDTAV-----GTPDYISPEVLKsqggDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhKNSLQFPDdv 255
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 368 TLSSDAKSLLSGLLIkDPNKRLGGGPDDakEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDE 437
Cdd:cd05596  256 EISKDAKSLICAFLT-DREVRLGRNGIE--EIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDD 322
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
151-410 2.94e-76

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: 239.30  E-value: 2.94e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRH-PFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATmKTFCGT 309
Cdd:cd05611   81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHN-KKFVGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDP 385
Cdd:cd05611  160 PDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEevkeFCSPEAVDLINRLLCMDP 239
                        250       260
                 ....*....|....*....|....*
gi 332078559 386 NKRLGGgpDDAKEIMRHSFFSGVNW 410
Cdd:cd05611  240 AKRLGA--NGYQEIKSHPFFKSINW 262
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-110 7.48e-76

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269947  Cd Length: 107  Bit Score: 232.52  E-value: 7.48e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   4 VTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVI 83
Cdd:cd01241    1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKPNQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTVI 80
                         90       100
                 ....*....|....*....|....*..
gi 332078559  84 ERTFHVDTPEEREEWTEAIQAVADRLQ 110
Cdd:cd01241   81 ERTFHVESEEEREEWMKAIQGVASSLK 107
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
146-456 1.15e-74

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: 238.98  E-value: 1.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK----------- 294
Cdd:cd05629   81 EFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsayy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 ----EG---------------------ITDAATMKTF-----------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 338
Cdd:cd05629  161 qkllQGksnknridnrnsvavdsinltMSSKDQIATWkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 339 MMCGRLPFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLSGlLIKDPNKRLGGGpdDAKEIMRHSFFSGVNWQDVy 414
Cdd:cd05629  241 CLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRR-LITNAENRLGRG--GAHEIKSHPFFRGVDWDTI- 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 332078559 415 dKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKCQQSD 456
Cdd:cd05629  317 -RQIRAPFIPQLKSITDTSYFPTDELEQVPEAPALKQAAPAQ 357
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
147-405 2.96e-74

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: 233.89  E-value: 2.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAK---DEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLK----EIDLSNmseKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERV----FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGI 297
Cdd:cd08215   77 VMEYADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKvlEST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDI-KFPRTLSSDAKSL 376
Cdd:cd08215  157 TDLA--KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYpPIPSQYSSELRDL 234
                        250       260
                 ....*....|....*....|....*....
gi 332078559 377 LSGLLIKDPNKRlgggPdDAKEIMRHSFF 405
Cdd:cd08215  235 VNSMLQKDPEKR----P-SANEILSSPFI 258
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
148-424 1.26e-71

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: 228.23  E-value: 1.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHL----SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd05608   83 MNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEDIKFPRTLSSDAKSLLSG 379
Cdd:cd05608  163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKSICEA 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 380 LLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05608  243 LLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
153-424 1.41e-71

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: 227.71  E-value: 1.41e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTE----SRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNErimlSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkegiTDAATMK--TF 306
Cdd:cd05606   81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA----CDFSKKKphAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQ---DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd05606  157 VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLYKLLKGHSPFRQHktkDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 332078559 383 KDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05606  237 RDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
148-424 3.85e-71

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: 226.83  E-value: 3.85e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd05630   82 MNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQTIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd05630  161 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRkkkiKREEVERLVKEVPEEYSEKFSPQARSLCSMLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 332078559 382 IKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05630  241 CKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
147-404 2.07e-70

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: 223.82  E-value: 2.07e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDAATMK 304
Cdd:cd14663   81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDGLLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIK 383
Cdd:cd14663  161 TTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDP 240
                        250       260
                 ....*....|....*....|.
gi 332078559 384 DPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14663  241 NPSTRI-----TVEQIMASPW 256
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
144-442 3.94e-70

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: 226.30  E-value: 3.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05610    2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--------- 294
Cdd:cd05610   82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnrelnm 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 -EGITDAATMKT-------------------------------------------FCGTPEYLAPEVLEDNDYGRAVDWW 330
Cdd:cd05610  162 mDILTTPSMAKPkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWW 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 331 GLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP---RTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFFSG 407
Cdd:cd05610  242 ALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAG-----LKELKQHPLFHG 316
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 332078559 408 VNWQDVYDKKlvPPFKPQVTSETDTRYFDEEFTAQ 442
Cdd:cd05610  317 VDWENLQNQT--MPFIPQPDDETDTSYFEARNNAQ 349
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
148-424 1.80e-69

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: 222.56  E-value: 1.80e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd05631   82 MNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGETVRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd05631  161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICRMLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 332078559 382 IKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05631  241 TKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
135-436 1.02e-68

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 222.55  E-value: 1.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 135 ASTTHHKRKT---MNDFDYLKLLGKGTFGKVILVREKaSGKY--YAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLT 209
Cdd:PTZ00426  16 DSTKEPKRKNkmkYEDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 210 SLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 289
Cdd:PTZ00426  95 NLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 290 FGLCKegITDAATMkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTL 369
Cdd:PTZ00426 175 FGFAK--VVDTRTY-TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFL 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 370 SSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFD 436
Cdd:PTZ00426 252 DNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
146-449 3.65e-68

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: 223.35  E-value: 3.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd05624  152 DYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQS 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFC-GTPEYLAPEVL---ED--NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR---TLSSDA 373
Cdd:cd05624  232 SVAvGTPDYISPEILqamEDgmGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhEERFQFPShvtDVSEEA 311
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 374 KSLLSgLLIKDPNKRLG-GGPDDAKeimRHSFFSGVNWQDVydKKLVPPFKPQVTSETDTRYFD-EEFTAQTITITPP 449
Cdd:cd05624  312 KDLIQ-RLICSRERRLGqNGIEDFK---KHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFDvDDDVLRNPEILPP 383
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
144-440 6.81e-66

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: 215.31  E-value: 6.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRH---PFLTSLKYSFQTKDR 220
Cdd:cd05633    3 TMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkegiTDA 300
Cdd:cd05633   83 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA----CDF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFC--GTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEDIKFPRTLSSDAK 374
Cdd:cd05633  159 SKKKPHAsvGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDSFSPELK 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 375 SLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP-----QVTSETDTRYFDEEFT 440
Cdd:cd05633  239 SLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 309
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
146-424 5.77e-65

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: 211.75  E-value: 5.77e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATM 303
Cdd:cd05632   82 TIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGESI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEDIKFPRTLSSDAKSLLSG 379
Cdd:cd05632  161 RGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICKM 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 380 LLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05632  241 LLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-388 1.04e-63

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: 206.84  E-value: 1.04e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLEN--EIAVLRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM---LDKDGHIKITDFGLCKegITDAATMK 304
Cdd:cd14083   83 VTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDSGVMS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGL 380
Cdd:cd14083  161 TACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSpywdDISDSAKDFIRHL 240

                 ....*...
gi 332078559 381 LIKDPNKR 388
Cdd:cd14083  241 MEKDPNKR 248
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
152-405 2.60e-63

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: 205.45  E-value: 2.60e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAH---TLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVK----EVELSGDSEEEleaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAATMKTF 306
Cdd:cd06606   82 PGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK--LFELILMEDI-KFPRTLSSDAKSLLSGLLIK 383
Cdd:cd06606  162 RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVaaLFKIGSSGEPpPIPEHLSEEAKDFLRKCLQR 241
                        250       260
                 ....*....|....*....|..
gi 332078559 384 DPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd06606  242 DPKKRP-----TADELLQHPFL 258
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
118-449 8.36e-63

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: 209.10  E-value: 8.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 118 NCSPTSQIDNIGEEEMDASTTHHKRKTM----NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHT 193
Cdd:cd05623   40 SNSPLRREKNILEYLEWAKPFTSKVKQMrlhkEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACF 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 194 LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDL 272
Cdd:cd05623  120 REERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDI 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 273 KLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC-GTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd05623  200 KPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAvGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPF 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 347 YNQDHEKLFELIL--MEDIKFPRTL---SSDAKSLLSGLLIKDPNKRLGGGPDDAKeimRHSFFSGVNWQDVydKKLVPP 421
Cdd:cd05623  280 YAESLVETYGKIMnhKERFQFPTQVtdvSENAKDLIRRLICSREHRLGQNGIEDFK---NHPFFVGIDWDNI--RNCEAP 354
                        330       340       350
                 ....*....|....*....|....*....|
gi 332078559 422 FKPQVTSETDTRYF--DEEFTAQTITITPP 449
Cdd:cd05623  355 YIPEVSSPTDTSNFdvDDDCLKNCETMPPP 384
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
154-403 1.48e-62

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: 202.12  E-value: 1.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAhtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEEL--LREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTP 310
Cdd:cd00180   79 KDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGTTPP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMmcgrlpfynqdheklfelilmedikfprtlsSDAKSLLSGLLIKDPNKRLg 390
Cdd:cd00180  159 YYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRP- 206
                        250
                 ....*....|...
gi 332078559 391 ggpdDAKEIMRHS 403
Cdd:cd00180  207 ----SAKELLEHL 215
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
154-405 7.45e-62

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: 202.01  E-value: 7.45e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKK-------EVIIAKDEVAHTL----TESRVLKNTRHPFLTSLkysFQ-----T 217
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKsrlrkrrEGKNDRGKIKNALddvrREIAIMKKLDHPNIVRL---YEviddpE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFF--HLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd14008   78 SDKLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDAATMKTFCGTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME--DIKFPRTLS 370
Cdd:cd14008  158 FEDGNDTLQKTAGTPAFLAPELCDGDSKtysGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQndEFPIPPELS 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 371 SDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14008  238 PELKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
148-388 1.78e-61

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: 200.69  E-value: 1.78e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNL-YSKDKLLQTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLsSDAKSLLSGLLIKDPN 386
Cdd:cd14073  162 GSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQP-SDASGLIRWMLTVNPK 240

                 ..
gi 332078559 387 KR 388
Cdd:cd14073  241 RR 242
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
146-390 2.20e-61

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: 200.56  E-value: 2.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMK-ILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKfIPKRGK--SEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGgELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd14002   79 TEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd14002  158 SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKD 237

                 ....*.
gi 332078559 385 PNKRLG 390
Cdd:cd14002  238 PSKRLS 243
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
148-402 7.88e-61

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: 199.09  E-value: 7.88e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAK-----DEVAhtltesrVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKehmieNEVA-------ILRRVKHPNIVQLIEEYDTDTELY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG----HIKITDFGLckegit 298
Cdd:cd14095   75 LVMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGL------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 dAATMK----TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDHEKLFELILMEDIKFPR----T 368
Cdd:cd14095  149 -ATEVKeplfTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSpywdN 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14095  228 ISDSAKDLISRMLVVDPEKRY-----SAGQVLDH 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
152-405 2.10e-60

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: 197.86  E-value: 2.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14081    7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG---LCKEGItdaaTMKTFCG 308
Cdd:cd14081   87 ELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGmasLQPEGS----LLETSCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 309 TPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNK 387
Cdd:cd14081  163 SPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEK 242
                        250
                 ....*....|....*...
gi 332078559 388 RLgggpdDAKEIMRHSFF 405
Cdd:cd14081  243 RI-----TIEEIKKHPWF 255
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
148-424 2.33e-60

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: 198.98  E-value: 2.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd05607   84 MNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKPITQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEDIKFPR-TLSSDAKSLLSGL 380
Cdd:cd05607  163 RAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFEHqNFTEEAKDICRLF 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 332078559 381 LIKDPNKRLGGGPDDaKEIMRHSFFSGVNWQDVYDKKLVPPFKP 424
Cdd:cd05607  243 LAKKPENRLGSRTND-DDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
125-437 5.29e-60

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: 201.77  E-value: 5.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 125 IDNIGEEEMDA-STTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNT 203
Cdd:cd05622   51 IDNFLSRYKDTiNKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 204 RHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG 283
Cdd:cd05622  131 NSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 284 HIKITDFGLC----KEGITDAATMktfCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 355
Cdd:cd05622  210 HLKLADFGTCmkmnKEGMVRCDTA---VGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTY 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 356 ELIL--MEDIKFPR--TLSSDAKSLLSGLLiKDPNKRLggGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETD 431
Cdd:cd05622  287 SKIMnhKNSLTFPDdnDISKEAKNLICAFL-TDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDID 363

                 ....*.
gi 332078559 432 TRYFDE 437
Cdd:cd05622  364 TSNFDD 369
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
147-437 2.84e-59

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: 199.07  E-value: 2.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05621   53 DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVME 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-KEGITDAATMKT 305
Cdd:cd05621  133 YMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCmKMDETGMVHCDT 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLL 377
Cdd:cd05621  212 AVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDdvEISKHAKNLI 291
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 378 SGLLiKDPNKRLggGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDE 437
Cdd:cd05621  292 CAFL-TDREVRL--GRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDD 348
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
152-405 5.35e-59

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: 194.41  E-value: 5.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14079    8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLcKEGITDAATMKTFCGTPE 311
Cdd:cd14079   88 ELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL-SNIMRDGEFLKTSCGSPN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLg 390
Cdd:cd14079  167 YAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRI- 245
                        250
                 ....*....|....*
gi 332078559 391 ggpdDAKEIMRHSFF 405
Cdd:cd14079  246 ----TIPEIRQHPWF 256
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
147-440 7.44e-59

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: 196.42  E-value: 7.44e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRH---PFLTSLKYSFQTKDRLCF 223
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkegiTDAATM 303
Cdd:cd14223   81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA----CDFSKK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFC--GTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEDIKFPRTLSSDAKSLL 377
Cdd:cd14223  157 KPHAsvGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTMAVELPDSFSPELRSLL 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 378 SGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP-----QVTSETDTRYFDEEFT 440
Cdd:cd14223  237 EGLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPprgevNAADAFDIGSFDEEDT 304
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
142-407 1.36e-57

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: 191.74  E-value: 1.36e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 142 RKTmndFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd14166    2 RET---FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEN---EIAVLKRIKHENIVTLEDIYESTTHY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKegIT 298
Cdd:cd14166   76 YLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--ME 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAK 374
Cdd:cd14166  154 QNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESpfwdDISESAK 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 332078559 375 SLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 407
Cdd:cd14166  234 DFIRHLLEKNPSKRY-----TCEKALSHPWIIG 261
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
152-405 2.98e-57

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: 189.69  E-value: 2.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPE 311
Cdd:cd14099   87 SLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTPN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTL--SSDAKSLLSGLLIKDPNKR 388
Cdd:cd14099  167 YIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQPDPTKR 246
                        250
                 ....*....|....*..
gi 332078559 389 LgggpdDAKEIMRHSFF 405
Cdd:cd14099  247 P-----SLDEILSHPFF 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
147-405 6.64e-57

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 188.95  E-value: 6.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESI---LNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd05122   78 FCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LSDGKTRNT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED---IKFPRTLSSDAKSLLSGLLI 382
Cdd:cd05122  157 FVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGppgLRNPKKWSKEFKDFLKKCLQ 236
                        250       260
                 ....*....|....*....|...
gi 332078559 383 KDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd05122  237 KDPEKRP-----TAEQLLKHPFI 254
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
151-401 9.23e-57

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: 188.56  E-value: 9.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK-EGITDAATMKTFCGT 309
Cdd:cd14014   85 GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARaLGDSGLTQTGSVLGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDP 385
Cdd:cd14014  165 PAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnpdVPPALDAIILRALAKDP 244
                        250
                 ....*....|....*.
gi 332078559 386 NKRlgggPDDAKEIMR 401
Cdd:cd14014  245 EER----PQSAAELLA 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
154-389 2.90e-56

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: 187.20  E-value: 2.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIiaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14078   11 IGSGGFAKVKLATHILTGEKVAIKIMDKKAL--GDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC---KEGITDAatMKTFCGTP 310
Cdd:cd14078   89 FDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCakpKGGMDHH--LETCCGSP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd14078  167 AYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRI 246
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
152-403 2.90e-56

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: 187.99  E-value: 2.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKE--VIIAKDEVAHT---LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14084   12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRkfTIGSRREINKPrniETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgITDAATM 303
Cdd:cd14084   92 LMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSKI-LGETSLM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLE---DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ-DHEKLFELILMEDIKF----PRTLSSDAKS 375
Cdd:cd14084  171 KTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKYTFipkaWKNVSEEAKD 250
                        250       260
                 ....*....|....*....|....*...
gi 332078559 376 LLSGLLIKDPNKRLgggpdDAKEIMRHS 403
Cdd:cd14084  251 LVKKMLVVDPSRRP-----SIEEALEHP 273
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-407 3.97e-56

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: 187.16  E-value: 3.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIEN--EIAVLHKIKHPNIVALDDIYESGGHLYLIMQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM---LDKDGHIKITDFGLCK-EGitDAATM 303
Cdd:cd14167   83 VSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKiEG--SGSVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSG 379
Cdd:cd14167  161 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKDFIQH 240
                        250       260
                 ....*....|....*....|....*...
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRHSFFSG 407
Cdd:cd14167  241 LMEKDPEKRF-----TCEQALQHPWIAG 263
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
148-388 1.30e-55

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: 185.54  E-value: 1.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKaSGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDaATMKTFC 307
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQD-KFLQTYC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPrTLSSDAKSLLSGLLIKDPN 386
Cdd:cd14161  163 GSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREP-TKPSDACGLIRWLLMVNPE 241

                 ..
gi 332078559 387 KR 388
Cdd:cd14161  242 RR 243
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
145-437 1.78e-55

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: 188.73  E-value: 1.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKeGITDAATMK 304
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCT-GLKKAHRTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TF------------------------------------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 348
Cdd:cd05627  160 FYrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 349 QDHEKLFELIL--MEDIKFPRT--LSSDAKSLLSGLLIkDPNKRLGGGPDDakEIMRHSFFSGVNWQDVYDKKLVPPFkp 424
Cdd:cd05627  240 ETPQETYRKVMnwKETLVFPPEvpISEKAKDLILRFCT-DAENRIGSNGVE--EIKSHPFFEGVDWEHIRERPAAIPI-- 314
                        330
                 ....*....|...
gi 332078559 425 QVTSETDTRYFDE 437
Cdd:cd05627  315 EIKSIDDTSNFDD 327
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
151-401 5.64e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 5.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK-TFCGT 309
Cdd:COG0515   92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTgTVVGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDA----KSLLSGLLIKDP 385
Cdd:COG0515  172 PGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLppalDAIVLRALAKDP 251
                        250
                 ....*....|....*.
gi 332078559 386 NKRlgggPDDAKEIMR 401
Cdd:COG0515  252 EER----YQSAAELAA 263
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
146-404 2.20e-53

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: 180.10  E-value: 2.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkeVIIAKDEVAHT---LTESRVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALK-----KIHVDGDEEFRkqlLRELKTLRSCESPYVVKCYGAFYKEGEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKeGITDAA 301
Cdd:cd06623   76 IVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISK-VLENTL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMK-TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFEL---ILMEDIKFPR--TLSSDAKS 375
Cdd:cd06623  155 DQCnTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELmqaICDGPPPSLPaeEFSPEFRD 234
                        250       260
                 ....*....|....*....|....*....
gi 332078559 376 LLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd06623  235 FISACLQKDPKKRP-----SAAELLQHPF 258
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
148-388 8.71e-53

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: 178.10  E-value: 8.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQL-NPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd14072   81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE-FTPGNKLDTFC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPN 386
Cdd:cd14072  160 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPS 239

                 ..
gi 332078559 387 KR 388
Cdd:cd14072  240 KR 241
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
147-404 1.38e-52

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: 178.02  E-value: 1.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEV------IIAKDEVAHTLTESRVLKNT------RHPFLTSLKYS 214
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASnaglkkEREKRLEKEISRDIRTIREAalssllNHPHICRLRDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 215 FQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLck 294
Cdd:cd14077   82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 EGITDAAT-MKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD 372
Cdd:cd14077  160 SNLYDPRRlLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSE 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 373 AKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 404
Cdd:cd14077  240 CKSLISRMLVVDPKKRAT-----LEQVLNHPW 266
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
147-437 1.74e-52

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: 181.01  E-value: 1.74e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKeGITDAATMKTF 306
Cdd:cd05628   82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT-GLKKAHRTEFY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 ------------------------------------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 350
Cdd:cd05628  161 rnlnhslpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSET 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 351 HEKLFELIL--MEDIKFPRT--LSSDAKSLLSGLLIKDPNKRlggGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFkpQV 426
Cdd:cd05628  241 PQETYKKVMnwKETLIFPPEvpISEKAKDLILRFCCEWEHRI---GAPGVEEIKTNPFFEGVDWEHIRERPAAIPI--EI 315
                        330
                 ....*....|.
gi 332078559 427 TSETDTRYFDE 437
Cdd:cd05628  316 KSIDDTSNFDE 326
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
151-405 4.07e-52

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: 176.60  E-value: 4.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILV--REKASGKYYAMKILKKEvIIAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14080    5 GKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKK-KAPKDFLEKFLPrELEILRKLRHPNIIQVYSIFERGSKVFIFMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-GITDAATM-KT 305
Cdd:cd14080   84 AEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLcPDDDGDVLsKT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT---LSSDAKSLLSGLL 381
Cdd:cd14080  164 FCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSvkkLSPECKDLIDQLL 243
                        250       260
                 ....*....|....*....|....
gi 332078559 382 IKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd14080  244 EPDPTKRAT-----IEEILNHPWL 262
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
153-405 6.68e-52

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: 176.39  E-value: 6.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKIL-----KKEVIIAKDEVAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14093   10 ILGRGVSSTVRRCIEKETGQEFAVKIIditgeKSSENEAEELREATRREIEILRQvSGHPNIIELHDVFESPTFIFLVFE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTF 306
Cdd:cd14093   90 LCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR-LDEGEKLREL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSL 376
Cdd:cd14093  169 CGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSpewdDISDTAKDL 248
                        250       260
                 ....*....|....*....|....*....
gi 332078559 377 LSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14093  249 ISKLLVVDPKKRL-----TAEEALEHPFF 272
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
144-402 7.47e-52

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 175.92  E-value: 7.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd14116    3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQL-EKAGVEHQLRrEVEIQSHLRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTDAAT 302
Cdd:cd14116   82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH--APSSR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd14116  160 RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK 239
                        250       260
                 ....*....|....*....|
gi 332078559 383 KDPNKRLgggpdDAKEIMRH 402
Cdd:cd14116  240 HNPSQRP-----MLREVLEH 254
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
147-402 7.51e-52

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: 176.13  E-value: 7.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQrEINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG--HIKITDFGLCKEgITDAATM 303
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV-IHTGTFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVL------EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlmEDIKFPR------TLSS 371
Cdd:cd14098  160 VTFCGTMAYLAPEILmskeqnLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRI--RKGRYTQpplvdfNISE 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332078559 372 DAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14098  238 EAIDFILRLLDVDPEKRM-----TAAQALDH 263
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
154-402 1.14e-51

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: 175.43  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKE------VIIAKDEVAhtltesrVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKINREkagssaVKLLEREVD-------ILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG-------HIKITDFGLC--KEGIT 298
Cdd:cd14097   82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvqKYGLG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAK 374
Cdd:cd14097  162 EDMLQET-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAK 240
                        250       260
                 ....*....|....*....|....*...
gi 332078559 375 SLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14097  241 NVLQQLLKVDPAHRM-----TASELLDN 263
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
148-436 1.20e-51

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: 179.05  E-value: 1.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05626    3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK------------- 294
Cdd:cd05626   83 IPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyqk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 ---------------------------EGITDAATMK-------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd05626  163 gshirqdsmepsdlwddvsncrcgdrlKTLEQRATKQhqrclahSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEML 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 341 CGRLPFYN-QDHEKLFELILMED-IKFPR--TLSSDAKSLLSGLLIKdPNKRLGGgpDDAKEIMRHSFFSGVNWQDvyDK 416
Cdd:cd05626  243 VGQPPFLApTPTETQLKVINWENtLHIPPqvKLSPEAVDLITKLCCS-AEERLGR--NGADDIKAHPFFSEVDFSS--DI 317
                        330       340
                 ....*....|....*....|.
gi 332078559 417 KLVP-PFKPQVTSETDTRYFD 436
Cdd:cd05626  318 RTQPaPYVPKISHPMDTSNFD 338
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
154-407 1.56e-51

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: 175.46  E-value: 1.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14169   11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVEN--EIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSE-DRTRFYGaEIVSALDYLHSGKIVYRDLKLENLMLD---KDGHIKITDFGLCKegITDAATMKTFCGT 309
Cdd:cd14169   89 FDRIIERGSYTEkDASQLIG-QVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQGMLSTACGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDP 385
Cdd:cd14169  166 PGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywdDISESAKDFIRHLLERDP 245
                        250       260
                 ....*....|....*....|..
gi 332078559 386 NKRLgggpdDAKEIMRHSFFSG 407
Cdd:cd14169  246 EKRF-----TCEQALQHPWISG 262
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
148-390 5.80e-51

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: 173.35  E-value: 5.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQL-DEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLcKEGITDAATMKTFC 307
Cdd:cd14071   81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF-SNFFKPGELLKTWC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPN 386
Cdd:cd14071  160 GSPPYAAPEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPS 239

                 ....
gi 332078559 387 KRLG 390
Cdd:cd14071  240 KRLT 243
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
141-421 8.42e-51

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: 8.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 141 KRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKD 219
Cdd:cd14117    1 RKFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQI-EKEGVEHQLRrEIEIQSHLRHPNILRLYNYFHDRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTD 299
Cdd:cd14117   80 RIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH--AP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSG 379
Cdd:cd14117  158 SLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISK 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRHSffsgvnWQDVYDKKLVPP 421
Cdd:cd14117  238 LLRYHPSERL-----PLKGVMEHP------WVKANSRRVLPP 268
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
146-402 1.55e-50

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: 173.39  E-value: 1.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVI-LVREKASGKYYAMKILKKEVI----IAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYkAVPLRNTGKPVAIKVVRKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-----------------DKD- 282
Cdd:cd14096   81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkaddDETk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 283 ---------------GHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 347
Cdd:cd14096  161 vdegefipgvggggiGIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFY 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 348 NQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14096  239 DESIETLTEKISRGDYTFLSpwwdEISKSAKDLISHLLTVDPAKRY-----DIDEFLAH 292
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
148-436 2.72e-50

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: 175.62  E-value: 2.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05625    3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-------------- 293
Cdd:cd05625   83 IPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqs 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 ----KEGITD-----------------------AATMKTFC------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd05625  163 gdhlRQDSMDfsnewgdpencrcgdrlkplerrAARQHQRClahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 341 CGRLPFYNQDHEKlfelILMEDIKFPRTLSSDAKSLL----SGLLIK---DPNKRLggGPDDAKEIMRHSFFSGVNWQDv 413
Cdd:cd05625  243 VGQPPFLAQTPLE----TQMKVINWQTSLHIPPQAKLspeaSDLIIKlcrGPEDRL--GKNGADEIKAHPFFKTIDFSS- 315
                        330       340
                 ....*....|....*....|....
gi 332078559 414 yDKKLVP-PFKPQVTSETDTRYFD 436
Cdd:cd05625  316 -DLRQQSaPYIPKITHPTDTSNFD 338
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-407 5.98e-50

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: 172.15  E-value: 5.98e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIEN--EIAVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCK-EGITDaaTM 303
Cdd:cd14168   90 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKmEGKGD--VM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSG 379
Cdd:cd14168  168 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywdDISDSAKDFIRN 247
                        250       260
                 ....*....|....*....|....*...
gi 332078559 380 LLIKDPNKRlgggpDDAKEIMRHSFFSG 407
Cdd:cd14168  248 LMEKDPNKR-----YTCEQALRHPWIAG 270
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
154-389 1.41e-49

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: 169.37  E-value: 1.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDK-KKEAVLR---EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD--KDGHIKITDFGLCKEgITDAATMKTFCGTPE 311
Cdd:cd14006   77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARK-LNPGEELKEIFGTPE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNK 387
Cdd:cd14006  156 FVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEyfssVSQEAKDFIRKLLVKEPRK 235

                 ..
gi 332078559 388 RL 389
Cdd:cd14006  236 RP 237
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
154-404 1.43e-49

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: 170.36  E-value: 1.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVIL-----VREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14076    9 LGEGEFGKVKLgwplpKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-GITDAATMKTFC 307
Cdd:cd14076   89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDLMSTSC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPE-VLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHE--------KLFELILMEDIKFPRTLSSDAKSLL 377
Cdd:cd14076  169 GSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPF-DDDPHnpngdnvpRLYRYICNTPLIFPEYVTPKARDLL 247
                        250       260
                 ....*....|....*....|....*..
gi 332078559 378 SGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14076  248 RRILVPNPRKRI-----RLSAIMRHAW 269
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
154-390 2.09e-49

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: 168.94  E-value: 2.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKdevahtLTES-----RVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKK------LQENleseiAILKSIKHPNIVRLYDVQKTEDFIYLVLEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH---IKITDFGLCKEgITDAATMKT 305
Cdd:cd14009   75 AGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARS-LQPASMAET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED--IKFP--RTLSSDAKSLLSGLL 381
Cdd:cd14009  154 LCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDavIPFPiaAQLSPDCKDLLRRLL 233

                 ....*....
gi 332078559 382 IKDPNKRLG 390
Cdd:cd14009  234 RRDPAERIS 242
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
147-390 3.19e-49

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: 168.72  E-value: 3.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKdEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQK-EREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSR----ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAt 302
Cdd:cd08530   80 YAPFGDLSKLISKrkkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLA- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 mKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEdiKFPR---TLSSDAKSLLSG 379
Cdd:cd08530  159 -KTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRG--KFPPippVYSQDLQQIIRS 235
                        250
                 ....*....|.
gi 332078559 380 LLIKDPNKRLG 390
Cdd:cd08530  236 LLQVNPKKRPS 246
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
152-405 1.82e-48

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: 167.09  E-value: 1.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVahtLT-----ESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14162    6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKK--APEDY---LQkflprEIEVIKGLKHPNLICFYEAIETTSRVYIIME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM--- 303
Cdd:cd14162   81 LAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGKpkl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 -KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlMEDIKFPR--TLSSDAKSLLSG 379
Cdd:cd14162  161 sETYCGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPKnpTVSEECKDLILR 239
                        250       260
                 ....*....|....*....|....*.
gi 332078559 380 LLIKDPnKRLgggpdDAKEIMRHSFF 405
Cdd:cd14162  240 MLSPVK-KRI-----TIEEIKRDPWF 259
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
148-402 2.40e-48

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: 166.55  E-value: 2.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC--RGREVCES--ELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH---IKITDFGLCKEGI-TDAATM 303
Cdd:cd14087   79 ATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKkGPNCLM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSG 379
Cdd:cd14087  159 KTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSgepwPSVSNLAKDFIDR 238
                        250       260
                 ....*....|....*....|...
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14087  239 LLTVNPGERL-----SATQALKH 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
147-401 7.16e-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: 165.28  E-value: 7.16e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKI--LKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISRMSRKMREEAID---EARVLSKLNSPYVIKYYDSFVDKGKLNIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAT 302
Cdd:cd08529   78 MEYAENGDLhsLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK-FPRTLSSDAKSLLSGLL 381
Cdd:cd08529  158 AQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCL 237
                        250       260
                 ....*....|....*....|
gi 332078559 382 IKDPNKRlgggpDDAKEIMR 401
Cdd:cd08529  238 TKDYRQR-----PDTTELLR 252
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
152-404 7.18e-48

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: 165.51  E-value: 7.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14185    6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIES--EILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCKEGItdaATMKTFC 307
Cdd:cd14185   84 DLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT---GPIFTVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEDIKF--P--RTLSSDAKSLLSGLL 381
Cdd:cd14185  161 GTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEFlpPywDNISEAAKDLISRLL 240
                        250       260
                 ....*....|....*....|...
gi 332078559 382 IKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14185  241 VVDPEKRY-----TAKQVLQHPW 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
154-404 1.05e-47

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: 164.82  E-value: 1.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKV-----ILVREKAsgkyyAMKILKKEVIiakDEVAHTLTESRV--LKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14075   10 LGSGNFSQVklgihQLTKEKV-----AIKILDKTKL---DQKTQRLLSREIssMEKLHHPNIIRLYEVVETLSKLHLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG---LCKEGitdaATM 303
Cdd:cd14075   82 YASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKRG----ETL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd14075  158 NTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQ 237
                        250       260
                 ....*....|....*....|..
gi 332078559 383 KDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14075  238 PVPSDRY-----SIDEIKNSEW 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
154-388 1.32e-47

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: 164.25  E-value: 1.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKasGKYYAMKILKKEVIIAKDEVAHtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEF-RREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEY 312
Cdd:cd13999   78 YDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPRW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 313 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIK----DPNKR 388
Cdd:cd13999  158 MAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF--KELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRcwneDPEKR 235
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
148-406 2.31e-47

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: 163.92  E-value: 2.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIK----KMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 306
Cdd:cd06614   78 MDGGSLTDIITQNPVrMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIK 383
Cdd:cd06614  158 VGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPEKWSPEFKDFLNKCLVK 237
                        250       260
                 ....*....|....*....|...
gi 332078559 384 DPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd06614  238 DPEKRP-----SAEELLQHPFLK 255
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
154-402 1.54e-46

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: 161.62  E-value: 1.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRN---EIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FfhlsrERVFSED------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH-IKITDFGLCKEGITDAaTMKT 305
Cdd:cd14103   78 F-----ERVVDDDfelterDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDK-KLKV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM-----EDIKFpRTLSSDAKSLLSGL 380
Cdd:cd14103  152 LFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRakwdfDDEAF-DDISDEAKDFISKL 230
                        250       260
                 ....*....|....*....|..
gi 332078559 381 LIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14103  231 LVKDPRKRM-----SAAQCLQH 247
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
154-404 6.43e-46

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: 161.05  E-value: 6.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd14086   88 FEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGFAGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPN 386
Cdd:cd14086  168 GYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLINQMLTVNPA 247
                        250
                 ....*....|....*...
gi 332078559 387 KRLGggpddAKEIMRHSF 404
Cdd:cd14086  248 KRIT-----AAEALKHPW 260
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-409 6.75e-46

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: 161.15  E-value: 6.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiakdEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV-----DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM---LDKDGHIKITDFGLCKEgITDAATMK 304
Cdd:cd14085   80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKI-VDQQVTMK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-LFELILMEDIKFPR----TLSSDAKSLLSG 379
Cdd:cd14085  159 TVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYDFVSpwwdDVSLNAKDLVKK 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRHSFFSGVN 409
Cdd:cd14085  239 LIVLDPKKRL-----TTQQALQHPWVTGKA 263
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
154-404 1.33e-45

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: 159.77  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKIlkkeviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKC------VDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL-CKEGITDAATMKTFC----- 307
Cdd:cd14010   82 ETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLaRREGEILKELFGQFSdegnv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 ----------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT-----LSSD 372
Cdd:cd14010  162 nkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPkvsskPSPD 241
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 373 AKSLLSGLLIKDPNKRLGGGpddakEIMRHSF 404
Cdd:cd14010  242 FKSLLKGLLEKDPAKRLSWD-----ELVKHPF 268
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
148-404 1.97e-45

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: 158.78  E-value: 1.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIakDE-VAHTLTESRVLkntRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKI--DEnVQREIINHRSL---RHPNIIRFKEVVLTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD--GHIKITDFGLCKEGITDAATmK 304
Cdd:cd14662   77 YAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVLHSQP-K 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEDIKFPR--TLSSDAKSLL 377
Cdd:cd14662  156 STVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFrktiQRIMSVQYKIPDyvRVSQDCRHLL 235
                        250       260
                 ....*....|....*....|....*..
gi 332078559 378 SGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14662  236 SRIFVANPAKRI-----TIPEIKNHPW 257
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
147-430 2.37e-45

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: 159.72  E-value: 2.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEI------EILLRYGQHPNIITLRDVYDDGNSVYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLEN-LMLDKDGH---IKITDFGLCKEGITDAAT 302
Cdd:cd14091   75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNiLYADESGDpesLRICDFGFAKQLRAENGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLfELIL--MEDIKFP------RTLSSDAK 374
Cdd:cd14091  155 LMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTP-EVILarIGSGKIDlsggnwDHVSDSAK 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 375 SLLSGLLIKDPNKRLgggpdDAKEIMRHSFFsgVNWQDVYDKKLVPPFKPQVTSET 430
Cdd:cd14091  234 DLVRKMLHVDPSQRP-----TAAQVLQHPWI--RNRDSLPQRQLTDPQDAALVKGA 282
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
154-389 7.87e-45

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: 157.91  E-value: 7.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESR--------------------VLKNTRHPFLTSLKY 213
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAGFFRRPPPRRkpgalgkpldpldrvyreiaILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 214 SFQ--TKDRLCFVMEYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd14118   82 VLDdpNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCKEGITDAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR- 367
Cdd:cd14118  161 VSNEFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPDd 240
                        250       260
                 ....*....|....*....|...
gi 332078559 368 -TLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd14118  241 pVVSEQLKDLILRMLDKNPSERI 263
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
148-388 3.41e-44

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: 155.65  E-value: 3.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiakDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DDVSkaHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKDGHIKITDFGLCKEGITdAATM 303
Cdd:cd14074   82 ELGDGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQP-GEKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILmeDIKF--PRTLSSDAKSLLSGL 380
Cdd:cd14074  161 ETSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIM--DCKYtvPAHVSPECKDLIRRM 238

                 ....*...
gi 332078559 381 LIKDPNKR 388
Cdd:cd14074  239 LIRDPKKR 246
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
152-405 7.81e-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: 154.70  E-value: 7.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFfHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP 310
Cdd:cd14189   87 SLA-HIWKARhTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLg 390
Cdd:cd14189  166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRL- 244
                        250
                 ....*....|....*
gi 332078559 391 ggpdDAKEIMRHSFF 405
Cdd:cd14189  245 ----TLDQILEHEFF 255
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
148-404 2.17e-43

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: 153.80  E-value: 2.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVI------IAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIER---EVSILRQVLHPNIITLHDVFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKD---GHIKITDFGLCKEgI 297
Cdd:cd14105   84 VLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLlDKNvpiPRIKLIDFGLAHK-I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEDIKFPRTlSSD 372
Cdd:cd14105  163 EDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavnydFDDEYFSNT-SEL 241
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 373 AKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14105  242 AKDFIRQLLVKDPRKRM-----TIQESLRHPW 268
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
151-405 4.65e-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: 152.39  E-value: 4.65e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKdevaHTLTESRVLKN----TRHPFLTSLKYSF--QTKDRLCFV 224
Cdd:cd05118    4 LRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPK----AALREIKLLKHlndvEGHPNIVKLLDVFehRGGNHLCLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVngGELFFHLSRE--RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKITDFGLCKEGITDAA 301
Cdd:cd05118   80 FELM--GMNLYELIKDypRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSFTSPPY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TmkTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHEkLFELILMEDIKFPrtlsSDAKSLLSGL 380
Cdd:cd05118  158 T--PYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGR-PLFPGDSE-VDQLAKIVRLLGT----PEALDLLSKM 229
                        250       260
                 ....*....|....*....|....*
gi 332078559 381 LIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd05118  230 LKYDPAKRI-----TASQALAHPYF 249
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
154-405 5.31e-43

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: 152.46  E-value: 5.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFG--KVILVREKASGKYYAMKILKKEVI--IAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQT-KDRLCFVMEYV 228
Cdd:cd13994    1 IGKGATSvvRIVTKKNPRSGVLYAVKEYRRRDDesKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkEGITDAATMKT--- 305
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA-EVFGMPAEKESpms 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 --FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFELILMEDIKFPRTLS-------SDAK 374
Cdd:cd13994  160 agLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrSAKKSDSAYKAYEKSGDFTNGPYEpienllpSECR 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332078559 375 SLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd13994  240 RLIYRMLHPDPEKRI-----TIDEALNDPWV 265
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
152-404 1.11e-42

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: 151.79  E-value: 1.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDE------VAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVK----EVSLVDDDkksresVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd06632   82 EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVL--EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLL 381
Cdd:cd06632  161 FKGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQyEGVAAIFKIGNSGELpPIPDHLSPDAKDFIRLCL 240
                        250       260
                 ....*....|....*....|...
gi 332078559 382 IKDPNKRlgggPdDAKEIMRHSF 404
Cdd:cd06632  241 QRDPEDR----P-TASQLLEHPF 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
152-405 1.67e-42

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: 150.97  E-value: 1.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVI--IAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPIntEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAATMKTFC 307
Cdd:cd06625   86 GGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSSTGMKSVT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFElILMEDIKF--PRTLSSDAKSLLSGLLIKD 384
Cdd:cd06625  166 GTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEfEPMAAIFK-IATQPTNPqlPPHVSEDARDFLSLIFVRN 244
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRlgggPdDAKEIMRHSFF 405
Cdd:cd06625  245 KKQR----P-SAEELLSHSFV 260
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
152-405 1.72e-42

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: 150.93  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPE 311
Cdd:cd14188   87 SMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTPN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRlgg 391
Cdd:cd14188  167 YLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDR--- 243
                        250
                 ....*....|....
gi 332078559 392 gpDDAKEIMRHSFF 405
Cdd:cd14188  244 --PSLDEIIRHDFF 255
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
152-402 2.62e-42

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: 150.90  E-value: 2.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVA-HTLTESrvlkntrHPFLTSLK--Y--SFQTKDRLCFVME 226
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNPK-ARREVElHWRASG-------CPHIVRIIdvYenTYQGRKCLLVVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSR--ERVFSEDRTrfygAEIV----SALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgI 297
Cdd:cd14089   79 CMEGGELFSRIQEraDSAFTEREA----AEIMrqigSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGFAKE-T 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEDIKFPRT----L 369
Cdd:cd14089  154 TTKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkKRIRNGQYEFPNPewsnV 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 332078559 370 SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14089  234 SEEAKDLIRGLLKTDPSERL-----TIEEVMNH 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
147-405 2.64e-42

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: 150.77  E-value: 2.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGK--------YYAMKILKKEVIIAkdevahtltESRVLKNTRHPFLTSLKYSFQTK 218
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKilvwkeidYGKMSEKEKQQLVS---------EVNILRELKHPNIVRYYDRIVDR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 D--RLCFVMEYVNGGEL---FFHLSRERVF-SEDRTRFYGAEIVSALDYLH-----SGKIVYRDLKLENLMLDKDGHIKI 287
Cdd:cd08217   72 AntTLYIVMEYCEGGDLaqlIKKCKKENQYiPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 288 TDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlmEDIKFPR 367
Cdd:cd08217  152 GDFGLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKI--KEGKFPR 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 332078559 368 ---TLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 405
Cdd:cd08217  230 ipsRYSSELNEVIKSMLNVDPDKR----P-SVEELLQLPLI 265
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
148-389 3.99e-42

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: 150.14  E-value: 3.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIaKDEVAHTLTESRVLkntRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKI-DENVQREIINHRSL---RHPNIVRFKEVILTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG--HIKITDFGLCKEGITDAATmKT 305
Cdd:cd14665   78 AAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQP-KS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYN----QDHEKLFELILMEDIKFPRT--LSSDAKSLLS 378
Cdd:cd14665  157 TVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYvhISPECRHLIS 236
                        250
                 ....*....|.
gi 332078559 379 GLLIKDPNKRL 389
Cdd:cd14665  237 RIFVADPATRI 247
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
152-389 4.12e-42

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: 151.68  E-value: 4.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEViiakdevaHTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14092   12 EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL--------DTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd14092   84 GELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARL-KPENQPLKTPC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF----YNQDHEKLFELILMEDIKFP----RTLSSDAKS 375
Cdd:cd14092  163 FTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDgeewKNVSSEAKS 242
                        250
                 ....*....|....
gi 332078559 376 LLSGLLIKDPNKRL 389
Cdd:cd14092  243 LIQGLLTVDPSKRL 256
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
154-404 1.21e-41

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: 148.73  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVI--IAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd08222    8 LGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLS----RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLdKDGHIKITDFGLCK--EGITDAATmkT 305
Cdd:cd08222   88 DLDDKISeykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRilMGTSDLAT--T 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd08222  165 FTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRMLNKD 244
                        250       260
                 ....*....|....*....|
gi 332078559 385 PNKRlgggpDDAKEIMRHSF 404
Cdd:cd08222  245 PALR-----PSAAEILKIPF 259
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
147-388 1.43e-41

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: 148.69  E-value: 1.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIA----KDEVAHTLT-ESRV---LKNTRHPFLTSLKYSFQTK 218
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvRDRKLGTVPlEIHIldtLNKRSHPNIVKLLDFFEDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 DRLCFVME-YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckegi 297
Cdd:cd14004   81 EFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 tDAATMK-----TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHeklfelILMEDIKFPRTLSS 371
Cdd:cd14004  155 -SAAYIKsgpfdTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSE 227
                        250
                 ....*....|....*..
gi 332078559 372 DAKSLLSGLLIKDPNKR 388
Cdd:cd14004  228 DLIDLISRMLNRDVGDR 244
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
152-405 1.91e-41

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: 148.14  E-value: 1.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd06627    6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKI-PKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLckegitdAATMK------- 304
Cdd:cd06627   85 SLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGV-------ATKLNevekden 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD-HEKLFELILMEDIKFPRTLSSDAKSLLSGLLIK 383
Cdd:cd06627  158 SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQpMAALFRIVQDDHPPLPENISPELRDFLLQCFQK 237
                        250       260
                 ....*....|....*....|..
gi 332078559 384 DPNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06627  238 DPTLR-----PSAKELLKHPWL 254
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
151-388 2.76e-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: 147.65  E-value: 2.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAK---DEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd08218    5 IKKIGEGSFGKALLVKSKEDGKQYVIK----EINISKmspKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd08218   81 CDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELART 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL-FELILMEDIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd08218  161 CIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLvLKIIRGSYPPVPSRYSYDLRSLVSQLFKRN 240

                 ....
gi 332078559 385 PNKR 388
Cdd:cd08218  241 PRDR 244
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
152-402 3.43e-41

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: 147.87  E-value: 3.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14184    7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIEN--EVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCK--EGitdaaTMKT 305
Cdd:cd14184   85 DLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATvvEG-----PLYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH--EKLFELILMEDIKFPR----TLSSDAKSLLSG 379
Cdd:cd14184  160 VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKLEFPSpywdNITDSAKELISH 239
                        250       260
                 ....*....|....*....|...
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14184  240 MLQVNVEARY-----TAEQILSH 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
146-405 4.34e-41

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: 147.49  E-value: 4.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLE--IDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAtmK 304
Cdd:cd06605   79 EYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLA--K 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK---LFEL---ILMEDikfPRTL-----SSDA 373
Cdd:cd06605  157 TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPsmmIFELlsyIVDEP---PPLLpsgkfSPDF 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 374 KSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06605  234 QDFVSQCLQKDPTER-----PSYKELMEHPFI 260
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
152-389 4.81e-41

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: 148.65  E-value: 4.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEViiakdeVAHTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRM------EANTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd14179   87 GELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPLKTPC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-------EKLFELILMEDIKFP----RTLSSDAKSL 376
Cdd:cd14179  167 FTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKsltctsaEEIMKKIKQGDFSFEgeawKNVSQEAKDL 246
                        250
                 ....*....|...
gi 332078559 377 LSGLLIKDPNKRL 389
Cdd:cd14179  247 IQGLLTVDPNKRI 259
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
148-405 5.45e-41

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: 147.81  E-value: 5.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILkkEVIIAK------DEV-AHTLTESRVLKNTR-HPFLTSLKYSFQTKD 219
Cdd:cd14181   12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKII--EVTAERlspeqlEEVrSSTLKEIHILRQVSgHPSIITLIDSYESST 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL-CKegIT 298
Cdd:cd14181   90 FIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsCH--LE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLE------DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----T 368
Cdd:cd14181  168 PGEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSpewdD 247
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14181  248 RSSTVKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
152-405 1.82e-40

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: 145.96  E-value: 1.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLK-NTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14106   14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRR-GQDCRNEILHEIAVLElCKDCPRVVNLHEVYETRSELILILELAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd14106   93 GELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRV-IGEGEEIREIL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTL----SSDAKSLLSGLLIK 383
Cdd:cd14106  172 GTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAIDFIKRLLVK 251
                        250       260
                 ....*....|....*....|..
gi 332078559 384 DPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14106  252 DPEKRL-----TAKECLEHPWL 268
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
154-405 2.22e-40

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: 145.69  E-value: 2.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEvIIAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKD-RLCFVMEYVNGG 231
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKIIDKK-KAPDDFVEKFLPrELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA----ATMKTFC 307
Cdd:cd14165   88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEngriVLSKTFC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYG-RAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT--LSSDAKSLLSGLLIKD 384
Cdd:cd14165  168 GSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSknLTSECKDLIYRLLQPD 247
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14165  248 VSQRL-----CIDEVLSHPWL 263
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
152-388 2.91e-40

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: 145.35  E-value: 2.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14070    8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRrEGRIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK----EGITDAatMKTF 306
Cdd:cd14070   88 GNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcagiLGYSDP--FSTQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF------YNQDHEKlfeLILMEDIKFPRTLSSDAKSLLSGL 380
Cdd:cd14070  166 CGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFtvepfsLRALHQK---MVDKEMNPLPTDLSPGAISFLRSL 242

                 ....*...
gi 332078559 381 LIKDPNKR 388
Cdd:cd14070  243 LEPDPLKR 250
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
147-389 3.32e-40

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: 145.00  E-value: 3.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd14186   82 MCHNGEMSRYLkNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 385
Cdd:cd14186  162 MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKNP 241

                 ....
gi 332078559 386 NKRL 389
Cdd:cd14186  242 ADRL 245
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
157-406 4.26e-40

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 145.00  E-value: 4.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 157 GTFGKVILVREKASGKYYAMKILKKEVIIAkDEVA-HTLtesrvLKNtrHPFLTSLKYSFQTKDRLCFVMEYVNGGELFF 235
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNA-IEPMvHQL-----MKD--NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 236 HLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKITDFGLCK----EGITDaatmktfcGTP 310
Cdd:PHA03390  99 LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKiigtPSCYD--------GTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELILME-----DIKFPRTLSSDAKSLLSGLLIKDP 385
Cdd:PHA03390 171 DYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE-DEDEELDLESLLkrqqkKLPFIKNVSKNANDFVQSMLKYNI 249
                        250       260
                 ....*....|....*....|.
gi 332078559 386 NKRLgggpDDAKEIMRHSFFS 406
Cdd:PHA03390 250 NYRL----TNYNEIIKHPFLK 266
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
146-404 6.25e-40

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: 144.69  E-value: 6.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE--AEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAAT-MK 304
Cdd:cd06609   79 EYCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQ-LTSTMSkRN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI------LMEDIKFprtlSSDAKSLLS 378
Cdd:cd06609  157 TFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIpknnppSLEGNKF----SKPFKDFVE 232
                        250       260
                 ....*....|....*....|....*.
gi 332078559 379 GLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd06609  233 LCLNKDPKERP-----SAKELLKHKF 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
148-405 1.12e-39

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: 144.29  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKIL--KKEVIIAKDEVAH----TLTESRVLKNTR-HPFLTSLKYSFQTKDR 220
Cdd:cd14182    5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVQElreaTLKEIDILRKVSgHPNIIQLKDTYETNTF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDA 300
Cdd:cd14182   85 FFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFCGTPEYLAPEVLE----DND--YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLS 370
Cdd:cd14182  164 EKLREVCGTPGYLAPEIIEcsmdDNHpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSpewdDRS 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 371 SDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14182  244 DTVKDLISRFLVVQPQKRY-----TAEEALAHPFF 273
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
152-404 1.14e-39

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: 143.60  E-value: 1.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILK---------KEViiaKDEVahtltesRVLKNTRHPFLTSLkYSFQT-KDRL 221
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRfqdndpktiKEI---ADEM-------KVLEGLDHPNLVRY-YGVEVhREEV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFfHLSRE-RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlCKEGITDA 300
Cdd:cd06626   75 YIFMEYCQEGTLE-ELLRHgRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKLKNN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATM------KTFCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHE--KLFELILMEDIKFPRTL 369
Cdd:cd06626  153 TTTmapgevNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWSELDNEwaIMYHVGMGHKPPIPDSL 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 370 --SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd06626  233 qlSPEGKDFLSRCLESDPKKRP-----TASELLDHPF 264
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
154-389 1.36e-39

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: 143.62  E-value: 1.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVI------IAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14194   13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIER---EVSILKEIQHPNVITLHEVYENKTDVILILEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDG---HIKITDFGLCKEgITDAATM 303
Cdd:cd14194   90 VAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMlLDRNVpkpRIKIIDFGLAHK-IDFGNEF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD----AKSLLSG 379
Cdd:cd14194  169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNtsalAKDFIRR 248
                        250
                 ....*....|
gi 332078559 380 LLIKDPNKRL 389
Cdd:cd14194  249 LLVKDPKKRM 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
154-405 1.71e-39

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: 142.78  E-value: 1.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVI--IAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQT--KDRLCFVMEYVN 229
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLrrIPNGE-ANVKREIQILRRLNHRNVIKLVDVLYNeeKQKLYMVMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GG-ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG----LCKegITDAATMK 304
Cdd:cd14119   80 GGlQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDL--FAEDDTCT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd14119  158 TSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLE 237
                        250       260
                 ....*....|....*....|...
gi 332078559 383 KDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14119  238 KDPEKRF-----TIEQIRQHPWF 255
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
148-404 1.84e-39

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: 143.17  E-value: 1.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVI------IAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd14196    7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHPNIITLHDVYENRTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDG---HIKITDFGLCKEgI 297
Cdd:cd14196   84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNIpipHIKLIDFGLAHE-I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD-HEKLFELILME---DIKFPRTLSSDA 373
Cdd:cd14196  163 EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTkQETLANITAVSydfDEEFFSHTSELA 242
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332078559 374 KSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14196  243 KDFIRKLLVKETRKRL-----TIQEALRHPW 268
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
154-417 4.01e-39

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: 142.57  E-value: 4.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAKIIQIE---SEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 -FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEY 312
Cdd:cd06611   90 dSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTPYW 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 313 LAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED---IKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd06611  170 MAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSSFNDFLKSCLVKD 249
                        250       260       270
                 ....*....|....*....|....*....|...
gi 332078559 385 PNKRLgggpdDAKEIMRHSFFSgvnwqDVYDKK 417
Cdd:cd06611  250 PDDRP-----TAAELLKHPFVS-----DQSDNK 272
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
148-404 5.04e-39

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: 142.09  E-value: 5.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMK-ILKKE----VIIAKDEVAhtltesrVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd14088    3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkFLKRDgrkvRKAAKNEIN-------ILKMVKHPNILQLVDVFETRKEYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD---KDGHIKITDFGLCKegiTD 299
Cdd:cd14088   76 IFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAK---LE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-------QDHEK-LFELILMEDIKFPR---- 367
Cdd:cd14088  153 NGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDeaeeddyENHDKnLFRKILAGDYEFDSpywd 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 368 TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14088  233 DISQAAKDLVTRLMEVEQDQRI-----TAEEAISHEW 264
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
153-402 5.64e-39

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: 142.55  E-value: 5.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKEViiakdevahTLTESRVLKNTR-------HPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHP---------GHSRSRVFREVEtlhqcqgHPNILQLIEYFEDDERFYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM---LDKDGHIKITDFGL---CKEGITD 299
Cdd:cd14090   80 EKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLgsgIKLSSTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTF-----CGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN--------------QD-HEKL 354
Cdd:cd14090  160 MTPVTTPelltpVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacQDcQELL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 355 FELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14090  240 FHSIQEGEYEFPEKewshISAEAKDLISHLLVRDASQRY-----TAEQVLQH 286
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
152-388 9.51e-39

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: 141.29  E-value: 9.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14183   12 RTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQN--EVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCKegITDAAtMKTFC 307
Cdd:cd14183   90 DLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT--VVDGP-LYTVC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLL 381
Cdd:cd14183  167 GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQVDFPSpywdNVSDSAKELITMML 246

                 ....*..
gi 332078559 382 IKDPNKR 388
Cdd:cd14183  247 QVDVDQR 253
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
146-405 1.50e-38

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: 140.48  E-value: 1.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKI---------LKKEVIIakdevahtltesrvLKNTRHPFLTSLKYSFQ 216
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVvpveedlqeIIKEISI--------------LKQCDSPYIVKYYGSYF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 217 TKDRLCFVMEYVNGGELFFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd06612   69 KNTDLWIVMEYCGAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQdheKLFELILMEDIKFPRTL------ 369
Cdd:cd06612  149 LTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDI---HPMRAIFMIPNKPPPTLsdpekw 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 332078559 370 SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06612  226 SPEFNDFVKKCLVKDPEER-----PSAIQLLQHPFI 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
150-405 2.17e-38

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 140.70  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAMKILKKEviIAKDEV-AHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd07829    1 YEKLekLGEGTYGVVYKAKDKKTGEIVALKKIRLD--NEEEGIpSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGgELFFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-GItdaaTMK 304
Cdd:cd07829   79 YCDQ-DLKKYLdKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAfGI----PLR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFcgTPE-----YLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE----KLFElIL--------------- 359
Cdd:cd07829  154 TY--THEvvtlwYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIdqlfKIFQ-ILgtpteeswpgvtklp 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 360 MEDIKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07829  231 DYKPTFPKwpkndlekvlpRLDPEGIDLLSKMLQYNPAKRI-----SAKEALKHPYF 282
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
154-389 2.26e-38

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: 139.73  E-value: 2.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVilvrekasgkYYAM-KILKKEVI----IAKDEVAHT-----LTESRVLKNTRHPFLTSLKySFQTKDRLCF 223
Cdd:cd14121    3 LGSGTYATV----------YKAYrKSGAREVVavkcVSKSSLNKAstenlLTEIELLKKLKHPHIVELK-DFQWDEEHIY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 -VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG--HIKITDFGLCKEgITDA 300
Cdd:cd14121   72 lIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQH-LKPN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED-IKFPRT--LSSDAKSLL 377
Cdd:cd14121  151 DEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLL 230
                        250
                 ....*....|..
gi 332078559 378 SGLLIKDPNKRL 389
Cdd:cd14121  231 LRLLQRDPDRRI 242
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
152-381 7.69e-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: 138.70  E-value: 7.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQE-SQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG---HIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd14082   88 MLEMILSSEKgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI-IGEKSFRRSVV 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDhEKLFELILMEDIKFPRT----LSSDAKSLLSGLL 381
Cdd:cd14082  167 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NED-EDINDQIQNAAFMYPPNpwkeISPDAIDLINNLL 242
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
148-388 8.31e-38

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: 138.55  E-value: 8.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAhTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEA-SKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI-KITDFGLCKEgITDAATMK 304
Cdd:cd08225   81 CDGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQ-LNDSMELA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd08225  160 YTCvGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEgNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFK 239

                 ....*.
gi 332078559 383 KDPNKR 388
Cdd:cd08225  240 VSPRDR 245
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
147-405 8.48e-38

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: 138.73  E-value: 8.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakDEVAhtltesrVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:cd06648    8 DLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMdlrkqqRRELLF--NEVV-------IMRDYQHPNIVEMYSSYLVGDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA 300
Cdd:cd06648   79 LWVVMEFLEGGALTDIVTHTRM-NEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI---LMEDIKFPRTLSSDAKSLL 377
Cdd:cd06648  158 PRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIrdnEPPKLKNLHKVSPRLRSFL 237
                        250       260
                 ....*....|....*....|....*...
gi 332078559 378 SGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd06648  238 DRMLVRDPAQRA-----TAAELLNHPFL 260
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
145-389 9.03e-38

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: 139.33  E-value: 9.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVII-----------------------AKDEVAHTLTESRVLK 201
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMrqagfprrppprgaraapegctqPRGPIERVYQEIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 202 NTRHPFLTSLKYSFQ--TKDRLCFVMEYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML 279
Cdd:cd14199   81 KLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 280 DKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLED---NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFE 356
Cdd:cd14199  160 GEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSEtrkIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 357 LILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd14199  240 KIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI 274
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
146-405 1.37e-37

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: 137.85  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKI-------------LKKEVIIAKdevahTLTESRVLKNTRHPFLTSLK 212
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdmkrapgdcpenIKKEVCIQK-----MLSHKNVVRFYGHRREGEFQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 213 YSFQtkdrlcfvmEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL 292
Cdd:cd14069   76 YLFL---------EYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 293 C-------KEGITDAAtmktfCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPfYNQDHEKLFE-LILMEDI 363
Cdd:cd14069  147 AtvfrykgKERLLNKM-----CGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELP-WDQPSDSCQEySDWKENK 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 332078559 364 KFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14069  221 KTYLTpwkkIDTAALSLLRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
154-390 3.05e-37

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: 137.77  E-value: 3.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVII----------------AKDEVAHTLT-------ESRVLKNTRHPFLTS 210
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLkqygfprrppprgskaAQGEQAKPLAplervyqEIAILKKLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 211 LKYSFQ--TKDRLCFVMEYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 288
Cdd:cd14200   88 LIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKF 365
Cdd:cd14200  167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQsfsGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEF 246
                        250       260
                 ....*....|....*....|....*..
gi 332078559 366 PR--TLSSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd14200  247 PEepEISEELKDLILKMLDKNPETRIT 273
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
143-388 3.61e-37

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: 136.99  E-value: 3.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 143 KTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd14187    4 RTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAT 302
Cdd:cd14187   84 VVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGER 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd14187  164 KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQ 243

                 ....*.
gi 332078559 383 KDPNKR 388
Cdd:cd14187  244 TDPTAR 249
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
147-405 4.37e-37

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: 136.67  E-value: 4.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLE---PGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 306
Cdd:cd06613   78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKfPRTL------SSDAKSLL 377
Cdd:cd06613  158 IGTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFD-PPKLkdkekwSPDFHDFI 236
                        250       260
                 ....*....|....*....|....*...
gi 332078559 378 SGLLIKDPNKRlgggPdDAKEIMRHSFF 405
Cdd:cd06613  237 KKCLTKNPKKR----P-TATKLLQHPFV 259
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
147-388 4.59e-37

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: 136.64  E-value: 4.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPK--SSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELF--FHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd08219   79 YCDGGDLMqkIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYAC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK-FPRTLSSDAKSLLSGLLIK 383
Cdd:cd08219  159 TYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKR 238

                 ....*
gi 332078559 384 DPNKR 388
Cdd:cd08219  239 NPRSR 243
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
154-404 5.79e-37

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: 136.34  E-value: 5.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKY-YAMK-ILKKEVIIAKDEVAhtlTESRVLKNTRHPFLTSLkYSFQ-TKDRLCFVMEYVNG 230
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPDLpVAIKcITKKNLSKSQNLLG---KEIKILKELSHENVVAL-LDCQeTSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG---------HIKITDFGLCK--EGITD 299
Cdd:cd14120   77 GDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARflQDGMM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMktfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL---FELILMEDIKFPRTLSSDAKSL 376
Cdd:cd14120  157 AATL---CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPSGTSPALKDL 233
                        250       260
                 ....*....|....*....|....*...
gi 332078559 377 LSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14120  234 LLGLLKRNPKDRI-----DFEDFFSHPF 256
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
154-405 2.75e-36

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: 134.67  E-value: 2.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakdevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06647   86 LAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd06647  165 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMD 244
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRLgggpdDAKEIMRHSFF 405
Cdd:cd06647  245 VEKRG-----SAKELLQHPFL 260
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
154-389 5.06e-36

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: 135.38  E-value: 5.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKK--EVIIAKDEVAHTLTESrvlkntrHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRrmEANTQREVAALRLCQS-------HPNIVALHEVLHDQYHTYLVMELLRGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH---IKITDFGLCKEGITDAATMKTFCG 308
Cdd:cd14180   87 ELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQTPCF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 309 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFEliLMEDIKFPR---------TLSSDAKS 375
Cdd:cd14180  167 TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfHNHAAD--IMHKIKEGDfslegeawkGVSEEAKD 244
                        250
                 ....*....|....
gi 332078559 376 LLSGLLIKDPNKRL 389
Cdd:cd14180  245 LVRGLLTVDPAKRL 258
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
147-404 5.28e-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: 133.72  E-value: 5.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLtESRVLKNTRHPFLTSLKYSFQTKDRLCF-VM 225
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQ-EAKLLSKLKHPNIVSYKESFEGEDGFLYiVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAA 301
Cdd:cd08223   80 GFCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARvlESSSDMA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGL 380
Cdd:cd08223  160 T--TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAM 237
                        250       260
                 ....*....|....*....|....
gi 332078559 381 LIKDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd08223  238 LHQDPEKR-----PSVKRILRQPY 256
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
146-405 1.80e-35

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: 133.21  E-value: 1.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKkevIIAKDEVAH--TLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFK---ESEDDEDVKktALREVKVLRQLRHENIVNLKEAFRRKGRLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK---EGITDA 300
Cdd:cd07833   78 VFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARaltARPASP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATmkTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEM---------------------MCGRLP------FYNQDH- 351
Cdd:cd07833  158 LT--DYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELldgeplfpgdsdidqlyliqkCLGPLPpshqelFSSNPRf 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 352 --EKLFELILMEDI--KFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07833  236 agVAFPEPSQPESLerRYPGKVSSPALDFLKACLRMDPKERL-----TCDELLQHPYF 288
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
152-405 1.89e-35

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: 131.98  E-value: 1.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMK-ILKKEVIIAKD---------EVAHTLTESrvlkNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd14005    6 DLLGKGGFGTVYSGVRIRDGLPVAVKfVPKSRVTEWAMingpvpvplEIALLLKAS----KPGVPGVIRLLDWYERPDGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGE-LFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD-GHIKITDFGlCKEGITD 299
Cdd:cd14005   82 LLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFG-CGALLKD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AAtMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQdheklfELILMEDIKFPRTLSSDAKSLLS 378
Cdd:cd14005  161 SV-YTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLFRPRLSKECCDLIS 233
                        250       260
                 ....*....|....*....|....*..
gi 332078559 379 GLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14005  234 RCLQFDPSKRP-----SLEQILSHPWF 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
154-389 2.44e-35

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: 132.43  E-value: 2.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVI------IAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrgVSREEIER---EVNILREIQHPNIITLHDIFENKTDVVLILEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDG---HIKITDFGLCKEgITDAATM 303
Cdd:cd14195   90 VSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMlLDKNVpnpRIKLIDFGIAHK-IEAGNEF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD----AKSLLSG 379
Cdd:cd14195  169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNtselAKDFIRR 248
                        250
                 ....*....|
gi 332078559 380 LLIKDPNKRL 389
Cdd:cd14195  249 LLVKDPKKRM 258
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
145-388 3.28e-35

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: 131.97  E-value: 3.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYL-----KLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTR-HPFLTSLKYSFQTK 218
Cdd:cd14198    2 MDNFNNFyiltsKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRR-GQDCRAEILHEIAVLELAKsNPRVVNLHEVYETT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 DRLCFVMEYVNGGELFFHL---SRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKD---GHIKITDFGL 292
Cdd:cd14198   81 SEIILILEYAAGGEIFNLCvpdLAEMVSENDIIRLI-RQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 293 CKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----T 368
Cdd:cd14198  160 SRK-IGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsS 238
                        250       260
                 ....*....|....*....|
gi 332078559 369 LSSDAKSLLSGLLIKDPNKR 388
Cdd:cd14198  239 VSQLATDFIQKLLVKNPEKR 258
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
154-405 3.35e-35

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: 132.54  E-value: 3.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakdevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06656   27 IGQGASGTVYTAIDIATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06656   98 LAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd06656  177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMD 256
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06656  257 VDRR-----GSAKELLQHPFL 272
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
147-394 3.70e-35

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: 131.86  E-value: 3.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASG-KYYAMK-ILKKEVIIAKDE------VAHTLTESRVLKNT-RHPFLTSLKYSFQT 217
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKSNGqTLLALKeINMTNPAFGRTEqerdksVGDIISEVNIIKEQlRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNG---GELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGK-IVYRDLKLENLMLDKDGHIKITDFGL 292
Cdd:cd08528   81 NDRLYIVMELIEGaplGEHFSSLKEKNEhFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 293 CKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY------------NQDHEKLFELILM 360
Cdd:cd08528  161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYstnmltlatkivEAEYEPLPEGMYS 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 332078559 361 EDIKFprtlssdaksLLSGLLIKDPNKRlgggPD 394
Cdd:cd08528  241 DDITF----------VIRSCLTPDPEAR----PD 260
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
146-405 6.02e-35

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: 130.94  E-value: 6.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVilvrekasgkYYAMKILKKEVIIAK--------DEVAHTLTESRVLKNTRHPFLTSLKYSFQT 217
Cdd:cd06610    1 DDYELIEVIGSGATAVV----------YAAYCLPKKEKVAIKridlekcqTSMDELRKEIQAMSQCNHPNVVSYYTSFVV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFfHLSRER----VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG-- 291
Cdd:cd06610   71 GDELWLVMPLLSGGSLL-DIMKSSyprgGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGvs 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 --LCKEGITDAATMKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDikfPRT 368
Cdd:cd06610  150 asLATGGDRTRKVRKTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQND---PPS 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 332078559 369 LSSDA---------KSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 405
Cdd:cd06610  227 LETGAdykkysksfRKMISLCLQKDPSKR----P-TAEELLKHKFF 267
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
152-392 6.36e-35

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 130.81  E-value: 6.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14190   10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMV---LLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFfhlsrERVFSEDR------TRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKDGH-IKITDFGLCKEgITDAATM 303
Cdd:cd14190   87 ELF-----ERIVDEDYhltevdAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARR-YNPREKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSG 379
Cdd:cd14190  161 KVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVSN 240
                        250
                 ....*....|...
gi 332078559 380 LLIKDPNKRLGGG 392
Cdd:cd14190  241 LIIKERSARMSAT 253
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
154-405 8.95e-35

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: 131.39  E-value: 8.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakdevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06654   28 IGQGASGTVYTAMDVATGQEVAIRQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06654   99 LAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd06654  178 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMD 257
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06654  258 VEKR-----GSAKELLQHQFL 273
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
147-405 9.20e-35

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: 130.52  E-value: 9.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKY-YAMKILKKEVIiAKDEvahTL--TESRVLKNTRHPFLTSLkYSFQT-KDRLC 222
Cdd:cd14202    3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNL-AKSQ---TLlgKEIKILKELKHENIVAL-YDFQEiANSVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG---------HIKITDFGLC 293
Cdd:cd14202   78 LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 K--EGITDAATMktfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEDIKFPRT 368
Cdd:cd14202  158 RylQNNMMAATL---CGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQAsspQDLRLFYEKNKSLSPNIPRE 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14202  235 TSSHLRQLLLGLLQRNQKDRM-----DFDEFFHHPFL 266
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
147-402 1.09e-34

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: 131.04  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKIL---KKeviiAKDEV---------AHTLTESRVLKNTrhpflTSLKYS 214
Cdd:cd14171    7 EVNWTQKLGTGISGPVRVCVKKSTGERFALKILldrPK----ARTEVrlhmmcsghPNIVQIYDVYANS-----VQFPGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 215 FQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDK---DGHIKITDFG 291
Cdd:cd14171   78 SSPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDnseDAPIKLCDFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCKEgitDAATMKTFCGTPEYLAPEVLEDND-----------------YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK- 353
Cdd:cd14171  158 FAKV---DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRt 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 354 ----LFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14171  235 itkdMKRKIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERM-----TIEEVLHH 286
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
152-389 2.41e-34

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: 129.34  E-value: 2.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKkEVIIAKDEVAHTLTESRVLKNTRhpFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALKLLY-DSPKARREVEHHWRASGGPHIVH--ILDVYENMHHGKRCLLIIMECMEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgITDAATMKTF 306
Cdd:cd14172   87 ELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKE-TTVQNALQTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEDIKFPR----TLSSDAKSLLS 378
Cdd:cd14172  166 CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQYGFPNpewaEVSEEAKQLIR 245
                        250
                 ....*....|.
gi 332078559 379 GLLIKDPNKRL 389
Cdd:cd14172  246 HLLKTDPTERM 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
154-388 3.80e-34

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: 128.94  E-value: 3.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEvIIAKDEVAHTLTesrVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNKK-LMKRDQVTHELG---VLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH---IKITDFGlckegitDAATMKT----- 305
Cdd:cd14113   91 LDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFG-------DAVQLNTtyyih 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 -FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGL 380
Cdd:cd14113  164 qLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFL 243

                 ....*...
gi 332078559 381 LIKDPNKR 388
Cdd:cd14113  244 LQMDPAKR 251
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
151-402 1.01e-33

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: 128.81  E-value: 1.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKIlkkeVIIAKDEVAHTLT------ESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd14094    8 CEVIGKGPFSVVRRCIHRETGQQFAVKI----VDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGMLYMV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRER----VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKE-- 295
Cdd:cd14094   84 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQlg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDAATMKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEDIKF-PR---TLSS 371
Cdd:cd14094  164 ESGLVAGGRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwsHISE 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332078559 372 DAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14094  241 SAKDLVRRMLMLDPAERI-----TVYEALNH 266
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
147-402 1.13e-33

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: 127.16  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQM-TKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI-KITDFGLCKEgITDAATM 303
Cdd:cd08220   80 YAPGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKI-LSSKSKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynqDHEKLFELIL--MEDIKFPRT--LSSDAKSLLSG 379
Cdd:cd08220  159 YTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAF---EAANLPALVLkiMRGTFAPISdrYSEELRHLILS 235
                        250       260
                 ....*....|....*....|...
gi 332078559 380 LLIKDPNKRlgggpDDAKEIMRH 402
Cdd:cd08220  236 MLHLDPNKR-----PTLSEIMAQ 253
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
148-389 1.39e-33

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 127.04  E-value: 1.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILK----KEVIIAKDEVAhtltesrVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKaysaKEKENIRQEIS-------IMNCLHHPKLVQCVDAFEEKANIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFfhlsrERVFSED------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDG-HIKITDFGLCKE 295
Cdd:cd14191   77 VLEMVSGGELF-----ERIIDEDfelterECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELIL----MEDIKFPRtLS 370
Cdd:cd14191  152 -LENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSatwdFDDEAFDE-IS 229
                        250
                 ....*....|....*....
gi 332078559 371 SDAKSLLSGLLIKDPNKRL 389
Cdd:cd14191  230 DDAKDFISNLLKKDMKARL 248
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
155-350 1.72e-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: 126.86  E-value: 1.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 155 GKGTFGKVILVREKASGKYYAMKIlkkeVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELF 234
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKI----VPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 235 FHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT-FCGTPEYL 313
Cdd:cd14111   88 HSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGrRTGTLEYM 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 332078559 314 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 350
Cdd:cd14111  168 APEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQD 204
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
152-405 2.11e-33

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 126.62  E-value: 2.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKN---EINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH-IKITDFGLCKEgITDAATMKTFCG 308
Cdd:cd14192   87 ELFDRITDESYqLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARR-YKPREKLKVNFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 309 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKD 384
Cdd:cd14192  166 TPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVKE 245
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14192  246 KSCRM-----SATQCLKHEWL 261
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
149-405 2.55e-33

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: 127.41  E-value: 2.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 149 DYLKLlGKGTFGKVILVREKASGKYYAMKI--LKKEviiAKDEVahTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd06659   25 NYVKI-GEGSTGVVCIAREKHSGRQVAVKMmdLRKQ---QRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLME 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 306
Cdd:cd06659   99 YLQGGALTDIVSQTR-LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIK 383
Cdd:cd06659  178 VGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKASPVLRDFLERMLVR 257
                        250       260
                 ....*....|....*....|..
gi 332078559 384 DPNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06659  258 DPQER-----ATAQELLDHPFL 274
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
154-405 2.63e-33

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: 127.53  E-value: 2.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakdevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06655   27 IGQGASGTVFTAIDVATGQEVAIKQInlqkqpKKELII---------NEILVMKELKNPNIVNFLDSFLVGDELFVVMEY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06655   98 LAGGSLT-DVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKD 384
Cdd:cd06655  177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLSPIFRDFLNRCLEMD 256
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRlgggpDDAKEIMRHSFF 405
Cdd:cd06655  257 VEKR-----GSAKELLQHPFL 272
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
152-404 2.80e-33

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: 127.07  E-value: 2.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEV---AHTLTESRVLKNtrhpfLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVfreVETLYQCQGNKN-----ILELIEFFEDDTRFYLVFEKL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGL---------CKEG 296
Cdd:cd14174   83 RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLgsgvklnsaCTPI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ITDAATmkTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ---------------DHEKLFE 356
Cdd:cd14174  163 TTPELT--TPCGSAEYMAPEVVEvftdeATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 357 LILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14174  241 SIQEGKYEFPDKdwshISSEAKDLISKLLVRDAKERL-----SAAQVLQHPW 287
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
154-413 4.40e-33

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: 126.68  E-value: 4.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14175    9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEI------EILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd14175   83 LDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCYT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFP------RTLSSDAKSLLSGLLI 382
Cdd:cd14175  163 ANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTrIGSGKFTlsggnwNTVSDAAKDLVSKMLH 242
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 332078559 383 KDPNKRLgggpdDAKEIMRHSFF--------SGVNWQDV 413
Cdd:cd14175  243 VDPHQRL-----TAKQVLQHPWItqkdklpqSQLNHQDV 276
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
152-402 5.34e-33

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: 125.80  E-value: 5.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14193   10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKN---EIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH-IKITDFGLCKEgITDAATMKTFCG 308
Cdd:cd14193   87 ELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARR-YKPREKLRVNFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 309 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEDIKFpRTLSSDAKSLLSGLLIK 383
Cdd:cd14193  166 TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILacqwdFEDEEF-ADISEEAKDFISKLLIK 244
                        250
                 ....*....|....*....
gi 332078559 384 DPNKRLgggpdDAKEIMRH 402
Cdd:cd14193  245 EKSWRM-----SASEALKH 258
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
148-389 8.26e-33

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: 125.00  E-value: 8.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14114    4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRK---EIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRE-RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD--KDGHIKITDFGLCKEgITDAATMK 304
Cdd:cd14114   81 LSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH-LDPKESVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGL 380
Cdd:cd14114  160 VTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIRKL 239

                 ....*....
gi 332078559 381 LIKDPNKRL 389
Cdd:cd14114  240 LLADPNKRM 248
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
151-358 9.36e-33

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: 124.97  E-value: 9.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   151 LKLLGKGTFGKVIL--VREKASGKYY--AMKILKKEV-IIAKDEVahtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:smart00221   4 GKKLGEGAFGEVYKgtLKGKGDGKEVevAVKTLKEDAsEQQIEEF---LREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   226 EYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATM 303
Cdd:smart00221  81 EYMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD-LYDDDYY 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559   304 KTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELI 358
Cdd:smart00221 160 KVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYL 217
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
151-405 1.01e-32

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: 125.34  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEviIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd07830    4 IKQLGDGTFGSVYLARNKETGELVAIKKMKKK--FYSWEECMNLREVKSLrKLNEHPNIVKLKEVFRENDELYFVFEYME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGelFFHLSRERV---FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTF 306
Cdd:cd07830   82 GN--LYQLMKDRKgkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLARE-IRSRPPYTDY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELI-------------LMED--IKF 365
Cdd:cd07830  159 VSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAELYTLR-PLFPGSSEidqlyKICSVLgtptkqdwpegykLASKlgFRF 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 366 PR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07830  238 PQfaptslhqlipNASPEAIDLIKDMLRWDPKKRP-----TASQALQHPYF 283
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
151-388 1.20e-32

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: 125.12  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKI--LKKEVIIAKDE--VAHTLTESRVLKNTRHPFLTSLKYSFQT-KDRLCFVM 225
Cdd:cd13990    5 LNLLGKGGFSEVYKAFDLVEQRYVACKIhqLNKDWSEEKKQnyIKHALREYEIHKSLDHPRIVKLYDVFEIdTDSFCTVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLDKD---GHIKITDFGLCK---EGI 297
Cdd:cd13990   85 EYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGnvsGEIKITDFGLSKimdDES 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATM---KTFCGTPEYLAPEVLEDNDYGR----AVDWWGLGVVMYEMMCGRLPF-YNQDHEK-LFELILME--DIKFP 366
Cdd:cd13990  165 YNSDGMeltSQGAGTYWYLPPECFVVGKTPPkissKVDVWSVGVIFYQMLYGRKPFgHNQSQEAiLEENTILKatEVEFP 244
                        250       260
                 ....*....|....*....|....
gi 332078559 367 R--TLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd13990  245 SkpVVSSEAKDFIRRCLTYRKEDR 268
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
140-409 1.26e-32

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: 125.53  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 140 HKRKTMNDFDYLKL---LGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQ 216
Cdd:cd06644    3 HVRRDLDPNEVWEIigeLGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEILATCNHPYIVKLLGAFY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 217 TKDRLCFVMEYVNGGEL-FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd06644   80 WDGKLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDAATMKTFCGTPEYLAPEV-----LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDikfPRTLS 370
Cdd:cd06644  160 NVKTLQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSE---PPTLS 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 371 SDAK------SLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSGVN 409
Cdd:cd06644  237 QPSKwsmefrDFLKTALDKHPETR-----PSAAQLLEHPFVSSVT 276
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
151-358 1.26e-32

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: 124.53  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  151 LKLLGKGTFGKV---ILVREKASGKY-YAMKILKKEVIiaKDEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDR-LCFVM 225
Cdd:pfam07714   4 GEKLGEGAFGEVykgTLKGEGENTKIkVAVKTLKEGAD--EEEREDFLEEASIMKKLDHPNIVKL-LGVCTQGEpLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  226 EYVNGGEL--FFHLSRERVFSEDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATM 303
Cdd:pfam07714  81 EYMPGGDLldFLRKHKRKLTLKDLLSM-ALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD-IYDDDYY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559  304 KTFCGTPE---YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:pfam07714 159 RKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFL 217
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
171-388 2.86e-32

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 128.21  E-value: 2.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 171 GKYYAMKILKKEVIIAKD-EVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLS---RERV-FSE 245
Cdd:PTZ00267  89 GSDPKEKVVAKFVMLNDErQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKqrlKEHLpFQE 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 246 DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATM---KTFCGTPEYLAPEVLEDND 322
Cdd:PTZ00267 169 YEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQ-YSDSVSLdvaSSFCGTPYYLAPELWERKR 247
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 323 YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK-FPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:PTZ00267 248 YSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALR 314
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
154-402 4.33e-32

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: 125.13  E-value: 4.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14176   27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI------EILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd14176  101 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFPRT------LSSDAKSLLSGLLI 382
Cdd:cd14176  181 ANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILArIGSGKFSLSggywnsVSDTAKDLVSKMLH 260
                        250       260
                 ....*....|....*....|
gi 332078559 383 KDPNKRLgggpdDAKEIMRH 402
Cdd:cd14176  261 VDPHQRL-----TAALVLRH 275
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
152-404 5.42e-32

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: 123.26  E-value: 5.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIA-------KDEVAHTLTESRVLKNTRHP-FLTSLKYSfQTKDRLCF 223
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSdradsrqKTVVDALKSEIDTLKDLDHPnIVQYLGFE-ETEDYFSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-----GIT 298
Cdd:cd06629   86 FLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKsddiyGNN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKtfcGTPEYLAPEVLEDND--YGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELI-------LMEDIKfprt 368
Cdd:cd06629  166 GATSMQ---GSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRPWSDDEAiAAMFKLGnkrsappVPEDVN---- 238
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 332078559 369 LSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSF 404
Cdd:cd06629  239 LSPEALDFLNACFAIDPRDR----P-TAAELLSHPF 269
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
152-358 7.82e-32

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: 122.26  E-value: 7.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILvrekasGKYY---------AMKILKKEviIAKDEVAHTLTESRVLKNTRHPFLTSLkYSFQT-KDRL 221
Cdd:cd00192    1 KKLGEGAFGEVYK------GKLKggdgktvdvAVKTLKED--ASESERKDFLKEARVMKKLGHPNVVRL-LGVCTeEEPL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHL--SRERVFSEDRTRF-------YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL 292
Cdd:cd00192   72 YLVMEYMEGGDLLDFLrkSRPVFPSPEPSTLslkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 293 CKEG-ITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd00192  152 SRDIyDDDYYRKKTGGKLPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYL 220
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
154-388 1.15e-31

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: 122.07  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESR-----VLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPQLreidlHRRVSRHPNIITLHDVFETEVAIYIVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVF---SEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKD-GHIKITDFGLckeGITDAATMK 304
Cdd:cd13993   88 PNGDLFEAITENRIYvgkTELIKNVF-LQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGL---ATTEKISMD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDND------YGRAVDWWGLGVVMYEMMCGRLPF------------YNQDHEKLFELILmedikfp 366
Cdd:cd13993  164 FGVGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWkiasesdpifydYYLNSPNLFDVIL------- 236
                        250       260
                 ....*....|....*....|..
gi 332078559 367 rTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd13993  237 -PMSDDFYNLLRQIFTVNPNNR 257
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
148-440 1.42e-31

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 123.40  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMK-ILK--KEVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCF- 223
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNvfDDLIDAK----RILREIKILRHLKHENIIGLLDILRPPSPEEFn 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 ----VMEYVnggELFFH--LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 297
Cdd:cd07834   78 dvyiVTELM---ETDLHkvIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TD-AATMKTfcgtpEYL------APEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------MED 362
Cdd:cd07834  155 PDeDKGFLT-----EYVvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVevlgtpsEED 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 363 IKFPR------------------------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFsgvnwQDVYDKKL 418
Cdd:cd07834  230 LKFISsekarnylkslpkkpkkplsevfpGASPEAIDLLEKMLVFNPKKRI-----TADEALAHPYL-----AQLHDPED 299
                        330       340
                 ....*....|....*....|..
gi 332078559 419 VPPFKPQVTSEtdtRYFDEEFT 440
Cdd:cd07834  300 EPVAKPPFDFP---FFDDEELT 318
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
164-389 1.47e-31

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: 122.51  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 164 LVREKASGKYYAMKILKKEViiaKDEVAHTLTESRVLKNTRHPFLT---------------------------SLKYSFQ 216
Cdd:cd13974   16 LARKEGTDDFYTLKILTLEE---KGEETQEDRQGKMLLHTEYSLLSllhdqdgvvhhhglfqdraceikedksSNVYTGR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 217 TKDRLCFVM-------------EYVNggeLFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG 283
Cdd:cd13974   93 VRKRLCLVLdclcahdfsdktaDLIN---LQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 284 H-IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME 361
Cdd:cd13974  170 RkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAA 249
                        250       260       270
                 ....*....|....*....|....*....|
gi 332078559 362 DIKFPRT--LSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd13974  250 EYTIPEDgrVSENTVCLIRKLLVLNPQKRL 279
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
154-404 1.61e-31

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: 122.43  E-value: 1.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEI------EILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd14178   85 LDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFPRT------LSSDAKSLLSGLLI 382
Cdd:cd14178  165 ANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILArIGSGKYALSggnwdsISDAAKDIVSKMLH 244
                        250       260
                 ....*....|....*....|..
gi 332078559 383 KDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14178  245 VDPHQRL-----TAPQVLRHPW 261
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
154-402 1.91e-31

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: 121.58  E-value: 1.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRK-GQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFFHL--SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD---GHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd14197   96 IFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRI-LKNSEELREIM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIK 383
Cdd:cd14197  175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEefehLSESAIDFIKTLLIK 254
                        250
                 ....*....|....*....
gi 332078559 384 DPNKRLgggpdDAKEIMRH 402
Cdd:cd14197  255 KPENRA-----TAEDCLKH 268
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
154-405 2.95e-31

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: 121.68  E-value: 2.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTL-TESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMD----LRKQQRRELLfNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEY 312
Cdd:cd06658  106 LTDIVTHTRM-NEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYW 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 313 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI---LMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd06658  185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIrdnLPPRVKDSHKVSSVLRGFLDLMLVREPSQRA 264
                        250
                 ....*....|....*.
gi 332078559 390 gggpdDAKEIMRHSFF 405
Cdd:cd06658  265 -----TAQELLQHPFL 275
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
154-403 3.31e-31

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: 120.51  E-value: 3.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKD---EVAHTLTESRvlkntrHPFLTS-LKYSFQTKDRLCFVMEYVN 229
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDflrEYNISLELSV------HPHIIKtYDVAFETEDYYVFAQEYAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLEN-LMLDKD-GHIKITDFGLC-KEGitdaATMKTF 306
Cdd:cd13987   75 YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDKDcRRVKLCDFGLTrRVG----STVKRV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGR-----AVDWWGLGVVMYEMMCGRLPFYNQD-HEKLFELIL--------MEDIKFpRTLSSD 372
Cdd:cd13987  151 SGTIPYTAPEVCEAKKNEGfvvdpSIDVWAFGVLLFCCLTGNFPWEKADsDDQFYEEFVrwqkrkntAVPSQW-RRFTPK 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332078559 373 AKSLLSGLLIKDPNKRlgGGPDDAKEIMRHS 403
Cdd:cd13987  230 ALRMFKKLLAPEPERR--CSIKEVFKYLGDR 258
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
148-405 4.49e-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: 121.23  E-value: 4.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDE--VAHTLTESRVLK---NTRHPFLTSLKYSFQTKDR-- 220
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVA---LKKVRVPLSEEgiPLSTIREIALLKqleSFEHPNVVRLLDVCHGPRTdr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 ---LCFVMEYVNGgELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKe 295
Cdd:cd07838   78 elkLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLAR- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gITDAATMKTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI------------ 358
Cdd:cd07838  156 -IYSFEMALTSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlGKIFDVIglpseeewprns 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 359 LMEDIKFPRTLSSDAKS-----------LLSGLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd07838  235 ALPRSSFPSYTPRPFKSfvpeideegldLLKKMLTFNPHKRIS-----AFEALQHPYF 287
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
152-389 4.91e-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: 121.29  E-value: 4.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKIL------KKEVII--AKDEVAHTLTESRVLKNTrhpfltslkysFQTKDRLCF 223
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLqdcpkaRREVELhwRASQCPHIVRIVDVYENL-----------YAGRKCLLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDK---DGHIKITDFGLCKEgIT 298
Cdd:cd14170   77 VMECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKE-TT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFELILMEDIKFPRT----LS 370
Cdd:cd14170  156 SHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPewseVS 235
                        250
                 ....*....|....*....
gi 332078559 371 SDAKSLLSGLLIKDPNKRL 389
Cdd:cd14170  236 EEVKMLIRNLLKTEPTQRM 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
148-406 5.75e-31

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: 121.14  E-value: 5.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKK-EVIIAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLgERKEAKDGINFTaLREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGG-ELFFHlSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd07841   82 EFMETDlEKVIK-DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNRKMT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCgRLPFYNQDHE-----KLFELI-------------LMEDIKF 365
Cdd:cd07841  161 HQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLL-RVPFLPGDSDidqlgKIFEALgtpteenwpgvtsLPDYVEF 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 366 -PRT----------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd07841  240 kPFPptplkqifpaASDDALDLLQRLLTLNPNKRI-----TARQALEHPYFS 286
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
153-404 6.91e-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: 119.95  E-value: 6.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMK--ILKKEVIIAKDEVAHTLT----ESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENKDRKKSMLDalqrEIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT- 305
Cdd:cd06628   87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNn 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 -----FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILMEDIKFPRTLSSDAKSLLSG 379
Cdd:cd06628  167 garpsLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASPTIPSNISSEARDFLEK 246
                        250       260
                 ....*....|....*....|....*
gi 332078559 380 LLIKDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06628  247 TFEIDHNKR-----PTADELLKHPF 266
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
148-423 7.34e-31

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: 120.16  E-value: 7.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06640    6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06640   84 LGGGSAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPfyNQDHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKD 384
Cdd:cd06640  163 GTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP--NSDMHPMRVLFLIPKNNPPTlvgDFSKPFKEFIDACLNKD 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 332078559 385 PNKRlgggpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 423
Cdd:cd06640  241 PSFR-----PTAKELLKHKFIVKNAKKTSYLTELIDRFK 274
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
145-409 9.53e-31

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: 120.13  E-value: 9.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKL---LGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd06643    1 LNPEDFWEIvgeLGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGEL-FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA 300
Cdd:cd06643   78 WILIEFCAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFCGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED---IKFPRTLSSD 372
Cdd:cd06643  158 QRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPE 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 373 AKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSGVN 409
Cdd:cd06643  238 FKDFLRKCLEKNVDARW-----TTSQLLQHPFVSVLV 269
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
148-404 1.01e-30

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: 119.89  E-value: 1.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRH-PFLTSLKY--SFQTKDRLCFV 224
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT--DDDDVSDIQKEVALLSQLKLgQPKNIIKYygSYLKGPSLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd06917   81 MDYCEGGSIR-TLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEDIKFPR----TLSSDAKSLLSG 379
Cdd:cd06917  160 TFVGTPYWMAPEViTEGKYYDTKADIWSLGITTYEMATGNPPY--SDVDALRAVMLIPKSKPPRlegnGYSPLLKEFVAA 237
                        250       260
                 ....*....|....*....|....*
gi 332078559 380 LLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd06917  238 CLDEEPKDRL-----SADELLKSKW 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
146-404 1.43e-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: 119.33  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTLTESRVLKN-TRHPFLTSLKYSFQTK------ 218
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEEEEIKLEINILRKfSNHPNIATFYGAFIKKdppggd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 DRLCFVMEYVNGG---ELF--FHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 293
Cdd:cd06608   82 DQLWLVMEYCGGGsvtDLVkgLRKKGKRL-KEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 KEgiTDAATMK--TFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED---I 363
Cdd:cd06608  161 AQ--LDSTLGRrnTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPpptL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 332078559 364 KFPRTLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSF 404
Cdd:cd06608  239 KSPEKWSKEFNDFISECLIKNYEQR----P-FTEELLEHPF 274
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
148-406 1.63e-30

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: 119.74  E-value: 1.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTL-TESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd06657   22 LDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMD----LRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVME 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 306
Cdd:cd06657   98 FLEGGALTDIVTHTRM-NEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI---LMEDIKFPRTLSSDAKSLLSGLLIK 383
Cdd:cd06657  177 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVR 256
                        250       260
                 ....*....|....*....|...
gi 332078559 384 DPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd06657  257 DPAQRA-----TAAELLKHPFLA 274
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
151-358 1.68e-30

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 118.79  E-value: 1.68e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   151 LKLLGKGTFGKVILvrekasGKYY----------AMKILKKEviiaKDEVAHT--LTESRVLKNTRHPFLTSLKYSFQTK 218
Cdd:smart00219   4 GKKLGEGAFGEVYK------GKLKgkggkkkvevAVKTLKED----ASEQQIEefLREARIMRKLDHPNVVKLLGVCTEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   219 DRLCFVMEYVNGGEL--FFHLSRERVFSEDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEG 296
Cdd:smart00219  74 EPLYIVMEYMEGGDLlsYLRKNRPKLSLSDLLSF-ALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559   297 ITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELI 358
Cdd:smart00219 153 YDDDYYRKRGGKLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYL 216
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
154-405 2.19e-30

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 118.97  E-value: 2.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKIL---KKEVIIAKDevahTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALKKValrKLEGGIPNQ----ALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYML 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGelffhLS-----RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegITDAATMK 304
Cdd:cd07832   84 SS-----LSevlrdEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR--LFSEEDPR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TF---CGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCG--------------------------------RLPFYN 348
Cdd:cd07832  157 LYshqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGsplfpgendieqlaivlrtlgtpnektwpeltSLPDYN 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 349 QDHEKLFELILMEDIkFPRTlSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd07832  237 KITFPESKGIRLEEI-FPDC-SPEAIDLLKGLLVYNPKKRLS-----AEEALRHPYF 286
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
146-388 2.49e-30

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: 118.55  E-value: 2.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd13996    6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR--LTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELfFHLSRERVFSEDRTRF----YGAEIVSALDYLHSGKIVYRDLKLENLMLDKD-GHIKITDFGLCK-----E 295
Cdd:cd13996   84 ELCEGGTL-RDWIDRRNSSSKNDRKlaleLFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATsignqK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDA---------ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlpfyNQDHEKLFELILMEDIKFP 366
Cdd:cd13996  163 RELNNlnnnnngntSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPF----KTAMERSTILTDLRNGILP 238
                        250       260
                 ....*....|....*....|....*
gi 332078559 367 RTLSS---DAKSLLSGLLIKDPNKR 388
Cdd:cd13996  239 ESFKAkhpKEADLIQSLLSKNPEER 263
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
152-402 2.99e-30

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: 118.98  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEViiakdevAHTltESRVLKNTR-------HPFLTSLKYSFQTKDRLCFV 224
Cdd:cd14173    8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRP-------GHS--RSRVFREVEmlyqcqgHRNVLELIEFFEEEDKFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI---KITDFGLcKEGI---T 298
Cdd:cd14173   79 FEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDL-GSGIklnS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMK-----TFCGTPEYLAPEVLEDND-----YGRAVDWWGLGVVMYEMMCGRLPFYNQ---------------DHEK 353
Cdd:cd14173  158 DCSPIStpellTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeacpaCQNM 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 354 LFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14173  238 LFESIQEGKYEFPEKdwahISCAAKDLISKLLVRDAKQRL-----SAAQVLQH 285
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
143-405 3.31e-30

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: 118.19  E-value: 3.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 143 KTMNDFDYLK--LLGKGTFGKVILVREKASGKY-YAMKILKKEVIiAKDEVAHTlTESRVLKNTRHPFLTSLKYSFQTKD 219
Cdd:cd14201    1 EVVGDFEYSRkdLVGHGAFAVVFKGRHRKKTDWeVAIKSINKKNL-SKSQILLG-KEIKILKELQHENIVALYDVQEMPN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG---------HIKITDF 290
Cdd:cd14201   79 SVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 291 GLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEDIKFPR 367
Cdd:cd14201  159 GFARY-LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQAnspQDLRMFYEKNKNLQPSIPR 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 368 TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14201  238 ETSPYLADLLLGLLQRNQKDRM-----DFEAFFSHPFL 270
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
147-388 4.08e-30

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: 117.48  E-value: 4.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGEL---FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkegitdaATM 303
Cdd:cd13997   81 LCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA-------TRL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFC----GTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCG-RLPFYNQDHEKLFELILmedIKFPR-TLSSDAKSL 376
Cdd:cd13997  154 ETSGdveeGDSRYLAPELLNENyTHLPKADIFSLGVTVYEAATGePLPRNGQQWQQLRQGKL---PLPPGlVLSQELTRL 230
                        250
                 ....*....|..
gi 332078559 377 LSGLLIKDPNKR 388
Cdd:cd13997  231 LKVMLDPDPTRR 242
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
154-404 4.15e-30

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: 117.89  E-value: 4.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKyyamKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQV----RIAIKEIPERDSREVQPLHEEIALhSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFfHLSRER----VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDK-DGHIKITDFGLCKE--GITDAAtmKT 305
Cdd:cd06624   92 LS-ALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRlaGINPCT--ET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGRLPFYN--QDHEKLFELILME---DIkfPRTLSSDAKSLLS 378
Cdd:cd06624  169 FTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIElgEPQAAMFKVGMFKihpEI--PESLSEEAKSFIL 246
                        250       260
                 ....*....|....*....|....*.
gi 332078559 379 GLLIKDPNKRLGggpddAKEIMRHSF 404
Cdd:cd06624  247 RCFEPDPDKRAT-----ASDLLQDPF 267
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
154-350 4.16e-30

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: 117.21  E-value: 4.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILvrekasGKYYAMKILKKEVIIAKDevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14059    1 LGSGAQGAVFL------GKFRGEEVAVKKVRDEKE------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYL 313
Cdd:cd14059   69 YEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKE-LSEKSTKMSFAGTVAWM 147
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 332078559 314 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 350
Cdd:cd14059  148 APEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVD 184
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
148-405 4.64e-30

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: 117.68  E-value: 4.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIP----LRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML--DKDGHIKITDFGLCKEgITDAATMKT 305
Cdd:cd14107   80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQE-ITPSEHQFS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE----KLFELILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd14107  159 KYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRatllNVAEGVVSWDTPEITHLSEDAKDFIKRVL 238
                        250       260
                 ....*....|....*....|....
gi 332078559 382 IKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd14107  239 QPDPEKRPS-----ASECLSHEWF 257
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
146-388 1.56e-29

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: 116.70  E-value: 1.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd14046    6 TDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK--LRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEG--------- 296
Cdd:cd14046   84 EYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNklnvelatq 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ----ITDAA-----TMKTFCGTPEYLAPEVLEDND--YGRAVDWWGLGVVMYEMMcgrLPFyNQDHEKLFEL-------I 358
Cdd:cd14046  164 dinkSTSAAlgssgDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPF-STGMERVQILtalrsvsI 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 332078559 359 LMEDiKFPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd14046  240 EFPP-DFDDNKHSKQAKLIRWLLNHDPAKR 268
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
152-404 2.00e-29

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: 115.91  E-value: 2.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILK--KEVIIAKDEVAHTLTESRVLKNTRHPFLTSLkYSF--QTKDR-LCFVME 226
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVQfdPESPETSKEVNALECEIQLLKNLLHERIVQY-YGClrDPQERtLSIFME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAAT-M 303
Cdd:cd06652   87 YMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlQTICLSGTgM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILM-EDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd06652  167 KSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEfEAMAAIFKIATQpTNPQLPAHVSDHCRDFLKRIF 246
                        250       260
                 ....*....|....*....|...
gi 332078559 382 IKDPNKrlgggpDDAKEIMRHSF 404
Cdd:cd06652  247 VEAKLR------PSADELLRHTF 263
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
150-405 2.07e-29

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: 116.24  E-value: 2.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAMKILKKEviiAKDE-VAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07835    1 YQKLekIGEGTYGVVYKARDKLTGEIVALKKIRLE---TEDEgVPSTaIREISLLKELNHPNIVRLLDVVHSENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGgELFFHLSRERVFSEDRTRF--YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-GItdaaT 302
Cdd:cd07835   78 EFLDL-DLKKYMDSSPLTGLDPPLIksYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfGV----P 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFcgTPE-----YLAPEV-LEDNDYGRAVDWWGLGVVMYEmMCGRLPFYNQDHE-----KLFELI------------L 359
Cdd:cd07835  153 VRTY--THEvvtlwYRAPEIlLGSKHYSTPVDIWSVGCIFAE-MVTRRPLFPGDSEidqlfRIFRTLgtpdedvwpgvtS 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 360 MEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07835  230 LPDYKptFPKwarqdlskvvpSLDEDGLDLLSQMLVYDPAKRI-----SAKAALQHPYF 283
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
154-406 2.12e-29

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: 116.65  E-value: 2.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14177   12 IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEI------EILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd14177   86 LDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGLLLTPCYT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 310 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFP------RTLSSDAKSLLSGLLI 382
Cdd:cd14177  166 ANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLrIGSGKFSlsggnwDTVSDAAKDLLSHMLH 245
                        250       260
                 ....*....|....*....|....
gi 332078559 383 KDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd14177  246 VDPHQRY-----TAEQVLKHSWIA 264
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
148-405 3.99e-29

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: 115.74  E-value: 3.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHT-LTESRVLKNTRHPFLTSL------KYSFQTKDR 220
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEGFPITaIREIKLLQKLDHPNVVRLkeivtsKGSAKYKGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYV----NGgelfFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLckeg 296
Cdd:cd07840   79 IYMVFEYMdhdlTG----LLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGL---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 itdAATM-KTFCG-------TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF-----YNQdHEKLFELI---- 358
Cdd:cd07840  151 ---ARPYtKENNAdytnrviTLWYRPPELLlGATRYGPEVDMWSVGCILAELFTGKPIFqgkteLEQ-LEKIFELCgspt 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 359 -----------LMEDIKFPRT------------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07840  227 eenwpgvsdlpWFENLKPKKPykrrlrevfknvIDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
154-346 1.20e-28

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: 114.47  E-value: 1.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLK-----YSFQTKDRLCFV-MEY 227
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARdvppeLEKLSPNDLPLLaMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFS---EDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKDGHI--KITDFGLCKEgITDAA 301
Cdd:cd13989   81 CSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRViyKLIDLGYAKE-LDQGS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 302 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd13989  160 LCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
151-405 1.26e-28

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: 114.52  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMK-ILK------KEVIIakdevahtltesrvLKNTRHPFLTSLKYSFQTKDR--- 220
Cdd:cd14137    9 EKVIGSGSFGVVYQAKLLETGEVVAIKkVLQdkryknRELQI--------------MRRLKHPNIVKLKYFFYSSGEkkd 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 ---LCFVMEYVNggelfFHLSRE-RVFSEDRTRF-------YGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKIT 288
Cdd:cd14137   75 evyLNLVMEYMP-----ETLYRViRHYSKNKQTIpiiyvklYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLC 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEGITDAATMKTFCgTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRlPFYNQDH--EKLFELILM----- 360
Cdd:cd14137  150 DFGSAKRLVPGEPNVSYIC-SRYYRAPELIFGAtDYTTAIDIWSAGCVLAELLLGQ-PLFPGESsvDQLVEIIKVlgtpt 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 361 -EDIK----------------------FPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14137  228 rEQIKamnpnytefkfpqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRL-----TALEALAHPFF 290
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
147-388 1.30e-28

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: 113.52  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKilKKEVIIAKDEVAHT--LTESRVLKNTRHPFLtsLKY--SFQTKDRLC 222
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALK--KVQIFEMMDAKARQdcLKEIDLLQQLNHPNI--IKYlaSFIENNELN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGEL---FFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd08224   77 IVLELADAGDLsrlIKHFKKQKRLIPERTIWkYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDHEKLFELIlmEDIKFP----RTLSSD 372
Cdd:cd08224  157 KTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYgeKMNLYSLCKKI--EKCEYPplpaDLYSQE 234
                        250
                 ....*....|....*.
gi 332078559 373 AKSLLSGLLIKDPNKR 388
Cdd:cd08224  235 LRDLVAACIQPDPEKR 250
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
147-388 1.43e-28

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: 114.07  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAmkilKKEVIIAKDEVAHT--LTESRVLKNTRHPFLTSLKYSFQTKD-RLCF 223
Cdd:cd06620    6 DLETLKDLGAGNGGSVSKVLHIPTGTIMA----KKVIHIDAKSSVRKqiLRELQILHECHSPYIVSFYGAFLNENnNIII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAt 302
Cdd:cd06620   82 CMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSIA- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 mKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDH------EKLFELI----------LMEDIK 364
Cdd:cd06620  161 -DTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAgsNDDDdgyngpMGILDLLqrivneppprLPKDRI 239
                        250       260
                 ....*....|....*....|....
gi 332078559 365 FPRtlssDAKSLLSGLLIKDPNKR 388
Cdd:cd06620  240 FPK----DLRDFVDRCLLKDPRER 259
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
148-423 2.22e-28

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: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06641   84 LGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR-TLSSDAKSLLSGLLIKDPN 386
Cdd:cd06641  163 GTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEgNYSKPLKEFVEACLNKEPS 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 387 KRlgggpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 423
Cdd:cd06641  243 FR-----PTAKELLKHKFILRNAKKTSYLTELIDRYK 274
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
148-404 3.06e-28

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: 112.84  E-value: 3.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd06642   84 LGGGSAL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDikfPRTL----SSDAKSLLSGLLIK 383
Cdd:cd06642  163 GTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNS---PPTLegqhSKPFKEFVEACLNK 239
                        250       260
                 ....*....|....*....|.
gi 332078559 384 DPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06642  240 DPRFR-----PTAKELLKHKF 255
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
152-404 7.53e-28

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: 111.66  E-value: 7.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKD------EVAHTLTESRVLKNTRHPFLTSLKYSFQ--TKDRLCF 223
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVK----QVPFDPDsqetskEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAA 301
Cdd:cd06653   84 FVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriQTICMSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 T-MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK--FPRTLSSDAKSLLS 378
Cdd:cd06653  164 TgIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKpqLPDGVSDACRDFLR 243
                        250       260
                 ....*....|....*....|....*.
gi 332078559 379 GLLIKDPNKRLgggpddAKEIMRHSF 404
Cdd:cd06653  244 QIFVEEKRRPT------AEFLLRHPF 263
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
152-404 1.02e-27

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: 111.33  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILK--KEVIIAKDEVAHTLTESRVLKNTRHPFLtsLKYSFQTKDR----LCFVM 225
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfdPESPETSKEVSALECEIQLLKNLQHERI--VQYYGCLRDRaektLTIFM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT---DAAT 302
Cdd:cd06651   91 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILM----EDIKFPRTLSSDAKSLLS 378
Cdd:cd06651  171 IRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW--AEYEAMAAIFKIatqpTNPQLPSHISEHARDFLG 248
                        250       260
                 ....*....|....*....|....*.
gi 332078559 379 GLLIKDPNKrlgggpDDAKEIMRHSF 404
Cdd:cd06651  249 CIFVEARHR------PSAEELLRHPF 268
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
152-405 1.04e-27

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: 111.59  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGK---GTFGKVILVREKASGKYYAMKILKKeVIIAKDEVAHtLTESRVLKN-TRHPFLTSLK---YSFQTKdRLCFV 224
Cdd:cd07831    2 KILGKigeGTFSEVLKAQSRKTGKYYAIKCMKK-HFKSLEQVNN-LREIQALRRlSPHPNILRLIevlFDRKTG-RLALV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDgHIKITDFGLCKeGITDAATMK 304
Cdd:cd07831   79 FELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCR-GIYSKPPYT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD--------HEKL----FELILME------DIKF 365
Cdd:cd07831  157 EYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNeldqiakiHDVLgtpdAEVLKKFrksrhmNYNF 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 366 PR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07831  237 PSkkgtglrkllpNASAEGLDLLKKLLAYDPDERI-----TAKQALRHPYF 282
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
152-405 1.75e-27

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: 110.60  E-value: 1.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILK--KEVIIAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEVVEAIReEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG-HIKITDFGLCKE---GITDAATMK 304
Cdd:cd06630   86 AGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARlasKGTGAGEFQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 -TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEDIKFPRTLSSDAKSLLS 378
Cdd:cd06630  166 gQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFkiasaTTPPPIPEHLSPGLRDVTL 245
                        250       260
                 ....*....|....*....|....*..
gi 332078559 379 GLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd06630  246 RCLELQPEDRPP-----ARELLKHPVF 267
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
141-406 1.96e-27

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: 110.52  E-value: 1.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 141 KRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:cd06645    6 RRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE---PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGEL--FFHLSRErvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd06645   83 LWICMEFCGGGSLqdIYHVTGP--LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEDIKF-PRTLSSDAK 374
Cdd:cd06645  161 TIAKRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMF--DLHPMRALFLMTKSNFqPPKLKDKMK 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 375 ------SLLSGLLIKDPNKRlgggpDDAKEIMRHSFFS 406
Cdd:cd06645  239 wsnsfhHFVKMALTKNPKKR-----PTAEKLLQHPFVT 271
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
154-388 2.04e-27

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: 110.05  E-value: 2.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEvIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK-MKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD---KDGHIKITDFGLCKEgITDAATMKTFCGTP 310
Cdd:cd14115   77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQ-ISGHRHVHHLLGNP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD----AKSLLSGLLIKDPN 386
Cdd:cd14115  156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDvsqaARDFINVILQEDPR 235

                 ..
gi 332078559 387 KR 388
Cdd:cd14115  236 RR 237
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
148-388 2.06e-27

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 110.33  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVilvREKASGKY---YAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQ-TKDRLCF 223
Cdd:cd14164    2 YTLGTTIGEGSFSKV---KLATSQKYcckVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVnGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG-HIKITDFGLCKEGITDAAT 302
Cdd:cd14164   79 VMEAA-ATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFynqdHEKLFELILMED--IKFPR--TLSSDAKSLL 377
Cdd:cd14164  158 STTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPF----DETNVRRLRLQQrgVLYPSgvALEEPCRALI 233
                        250
                 ....*....|.
gi 332078559 378 SGLLIKDPNKR 388
Cdd:cd14164  234 RTLLQFNPSTR 244
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
141-404 3.18e-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: 110.12  E-value: 3.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 141 KRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:cd06646    4 RRNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLE---PGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGEL--FFHLSRErvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd06646   81 LWICMEYCGGGSLqdIYHVTGP--LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEV--LEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEDIKF-PRTL----- 369
Cdd:cd06646  159 TIAKRKSFIGTPYWMAPEVaaVEKNgGYNQLCDIWAVGITAIELAELQPPMF--DLHPMRALFLMSKSNFqPPKLkdktk 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 332078559 370 -SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06646  237 wSSTFHNFVKISLTKNPKKR-----PTAERLLTHLF 267
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
121-407 3.26e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 111.84  E-value: 3.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 121 PTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHTLT-ESRV 199
Cdd:PLN00034  49 PPSSSSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN---HEDTVRRQICrEIEI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 200 LKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL-FFHLSRERVFSeDRTRfygaEIVSALDYLHSGKIVYRDLKLENLM 278
Cdd:PLN00034 126 LRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLeGTHIADEQFLA-DVAR----QILSGIAYLHRRHIVHRDIKPSNLL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 279 LDKDGHIKITDFGLckeGITDAATM---KTFCGTPEYLAPEV----LEDNDY-GRAVDWWGLGVVMYEMMCGRLPF---Y 347
Cdd:PLN00034 201 INSAKNVKIADFGV---SRILAQTMdpcNSSVGTIAYMSPERintdLNHGAYdGYAGDIWSLGVSILEFYLGRFPFgvgR 277
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 348 NQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 407
Cdd:PLN00034 278 QGDWASLMCAICMSQPpEAPATASREFRHFISCCLQREPAKRW-----SAMQLLQHPFILR 333
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
151-406 4.60e-27

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: 111.23  E-value: 4.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKK---EVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKDRL------ 221
Cdd:cd07851   20 LSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfqSAIHAK----RTYRELRLLKHMKHENVIGLLDVFTPASSLedfqdv 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVnGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTDaA 301
Cdd:cd07851   96 YLVTHLM-GADLN-NIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARH--TD-D 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH---------------EKLFELILMEDIK- 364
Cdd:cd07851  171 EMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHidqlkrimnlvgtpdEELLKKISSESARn 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 365 FPRTL---------------SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd07851  251 YIQSLpqmpkkdfkevfsgaNPLAIDLLEKMLVLDPDKRI-----TAAEALAHPYLA 302
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
153-404 2.13e-26

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: 107.52  E-value: 2.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVI--LVREkasGKYYAMKILK---KEVIIAKDEVAHTLTESRVLKNTRHP----FL-TSLKYSFqtkdrLC 222
Cdd:cd06631    8 VLGKGAYGTVYcgLTST---GQLIAVKQVEldtSDKEKAEKEYEKLQEEVDLLKTLKHVnivgYLgTCLEDNV-----VS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG----LCKEG-- 296
Cdd:cd06631   80 IFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLss 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP----------FYNQDHEKLFElilmediKFP 366
Cdd:cd06631  160 GSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFAIGSGRKPVP-------RLP 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 367 RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd06631  233 DKFSPEARDFVHACLTRDQDERP-----SAEQLLKHPF 265
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
157-405 2.36e-26

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: 107.25  E-value: 2.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 157 GTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahTLTESRVlkntrhPFLTSLKYSFQTKDRLCFVMEYVNGGELFFH 236
Cdd:cd05576   10 GVIDKVLLVMDTRTQETFILKGLRKSSEYSRERK--TIIPRCV------PNMVCLRKYIISEESVFLVLQHAEGGKLWSY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 237 LSR-------ERVFSE------DRTRFY---------GAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK 294
Cdd:cd05576   82 LSKflndkeiHQLFADlderlaAASRFYipeeciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 EgITDA----ATMKTFCgtpeylAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL-----PFYNQDHEKLfelilmediKF 365
Cdd:cd05576  162 E-VEDScdsdAIENMYC------APEVGGISEETEACDWWSLGALLFELLTGKAlvechPAGINTHTTL---------NI 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 332078559 366 PRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFF 405
Cdd:cd05576  226 PEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
144-388 2.39e-26

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: 107.31  E-value: 2.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAhTLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd14110    1 TEKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYK---PEDKQL-VLREYQVLRRLSHPRIAQLHSAYLSPRHLVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd14110   77 IEELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCG-TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT---LSSDAKSLLSG 379
Cdd:cd14110  157 TDKKGdYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGAVNFLKS 236

                 ....*....
gi 332078559 380 LLIKDPNKR 388
Cdd:cd14110  237 TLCAKPWGR 245
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
153-346 3.01e-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: 107.09  E-value: 3.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVIlvREKASGKYYAMKILKKEViiaKDEVAHTL----TESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14061    1 VIGVGGFGKVY--RGIWRGEEVAVKAARQDP---DEDISVTLenvrQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGK---IVYRDLKLENLMLDK--------DGHIKITDFGLCKEgI 297
Cdd:cd14061   76 RGGALNRVLAGRKI-PPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLARE-W 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 332078559 298 TDAATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14061  154 HKTTRMSA-AGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
152-384 3.28e-26

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: 107.00  E-value: 3.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKK----EVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKD-RLCFVME 226
Cdd:cd14163    6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKsggpEEFIQR----FLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLdKDGHIKITDFGLCKEGITDAATM-KT 305
Cdd:cd14163   82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGGRELsQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFeLILMEDIKFPRTL--SSDAKSLLSGLLI 382
Cdd:cd14163  161 FCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKML-CQQQKGVSLPGHLgvSRTCQDLLKRLLE 239

                 ..
gi 332078559 383 KD 384
Cdd:cd14163  240 PD 241
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
151-405 3.69e-26

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: 106.58  E-value: 3.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLK--NTRHP----FLTSLKYSFQTKDRLCFV 224
Cdd:cd14133    4 LEVLGKGTFGQVVKCYDLLTGEEVALKIIKNN----KDYLDQSLDEIRLLEllNKKDKadkyHIVRLKDVFYFKNHLCIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVnGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML--DKDGHIKITDFGLCKEgITDA 300
Cdd:cd14133   80 FELL-SQNLyeFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCF-LTQR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKS----- 375
Cdd:cd14133  158 LY--SYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKAddelf 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 376 --LLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14133  236 vdFLKKLLEIDPKERP-----TASQALSHPWL 262
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
151-388 8.99e-26

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 105.59  E-value: 8.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGkyyaMKILKKEVIIAK---DEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd08221    5 VRVLGRGAFGEAVLYRKTEDN----SLVVWKEVNLSRlseKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd08221   81 CNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEDIKFprtlSSDAKSLLSGL 380
Cdd:cd08221  161 IVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVqgeyeDIDEQY----SEEIIQLVHDC 236

                 ....*...
gi 332078559 381 LIKDPNKR 388
Cdd:cd08221  237 LHQDPEDR 244
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
143-405 1.59e-25

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: 106.30  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 143 KTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTK--D 219
Cdd:cd07845    4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISsLREITLLLNLRHPNIVELKEVVVGKhlD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNG--GELFFHLSRErvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 297
Cdd:cd07845   82 SIFLVMEYCEQdlASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI------------------ 358
Cdd:cd07845  160 LPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIiqllgtpnesiwpgfsdl 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 359 -LMEDIKFPRT-----------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07845  240 pLVGKFTLPKQpynnlkhkfpwLSEAGLRLLNFLLMYDPKKRA-----TAEEALESSYF 293
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
148-405 1.70e-25

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: 105.66  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKilKKEVIIAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALK--KIRLDTETEGVPSTaIREISLLKELNHPNIVKLLDVIHTENKLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVN-----------GGELFFHLSRERVFsedrtrfygaEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd07860   80 FLHqdlkkfmdasaLTGIPLPLIKSYLF----------QLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDAATMKTFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELIL-------------- 359
Cdd:cd07860  150 FGVPVRTYTHEVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPgDSEIDQLFRIFRtlgtpdevvwpgvt 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 360 -MEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07860  230 sMPDYKpsFPKwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRI-----SAKAALAHPFF 284
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
144-405 2.68e-25

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: 105.47  E-value: 2.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilKKEVIIAKDEVAHT-LTESRVLKNTRHPFLTSL------KYSFQ 216
Cdd:cd07866    6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALK--KILMHNEKDGFPITaLREIKILKKLKHPNVVPLidmaveRPDKS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 217 TKDRLCF--VMEYVNGgELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 293
Cdd:cd07866   84 KRKRGSVymVTPYMDH-DLSGLLENPSVkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 KeGITDAATMKTFCGTPE------------YLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFY------NQDHeKL 354
Cdd:cd07866  163 R-PYDGPPPNPKGGGGGGtrkytnlvvtrwYRPPElLLGERRYTTAVDIWGIGCVFAEMFTRR-PILqgksdiDQLH-LI 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 355 FEL------ILM---------EDIKF----PRTLSS-------DAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07866  240 FKLcgtpteETWpgwrslpgcEGVHSftnyPRTLEErfgklgpEGLDLLSKLLSLDPYKRL-----TASDALEHPYF 311
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
148-388 2.99e-25

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: 103.93  E-value: 2.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDR-KRKLEEVERHEKlGEHPNCVRFIKAWEEKGILYIQTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVnGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC----KEGITDAAT 302
Cdd:cd14050   82 LC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVveldKEDIHDAQE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 mktfcGTPEYLAPEVLeDNDYGRAVDWWGLGVVMYEMMCG-RLPFYNQDHEKLFELILMEDikFPRTLSSDAKSLLSGLL 381
Cdd:cd14050  161 -----GDPRYMAPELL-QGSFTKAADIFSLGITILELACNlELPSGGDGWHQLRQGYLPEE--FTAGLSPELRSIIKLMM 232

                 ....*..
gi 332078559 382 IKDPNKR 388
Cdd:cd14050  233 DPDPERR 239
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
154-348 3.08e-25

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: 104.28  E-value: 3.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKaSGKYYAMKILKKEVIIAKDEVAhtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASKKEF--LTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSR---ERVFS-EDRTRFyGAEIVSALDYLHSG---KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT- 305
Cdd:cd14066   78 EDRLHChkgSPPLPwPQRLKI-AKGIARGLEYLHEEcppPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTs 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332078559 306 -FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 348
Cdd:cd14066  157 aVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDE 200
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
154-398 4.01e-25

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: 104.61  E-value: 4.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIA-KDEVAHtltESRVLKNTRHPFLTSLK-----YSFQTKDRLCFVMEY 227
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKnKDRWCH---EIQIMKKLNHPNVVKACdvpeeMNFLVNDVPLLAMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERV---FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKDGHI--KITDFGLCKEgITDAA 301
Cdd:cd14039   78 CSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKD-LDQGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-------------NQDHEKLFELILME-DIKF-- 365
Cdd:cd14039  157 LCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLhnlqpftwhekikKKDPKHIFAVEEMNgEVRFst 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 332078559 366 ----PRTLSS----DAKSLLSGLLIKDPNKRLGGGPDDAKE 398
Cdd:cd14039  237 hlpqPNNLCSlivePMEGWLQLMLNWDPVQRGGGLDTDSKQ 277
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
145-388 4.32e-25

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: 103.95  E-value: 4.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilKKEVIIAKDEVAHT--LTESRVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALK--KVQIFEMMDAKARQdcVKEIDLLKQLNHPNVIKYLDSFIEDNELN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGEL---FFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd08228   79 IVLELADAGDLsqmIKYFKKQKRLIPERTVWkYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELIL-MEDIKFP----RTLSSDA 373
Cdd:cd08228  159 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLFSLCQkIEQCDYPplptEHYSEKL 237
                        250
                 ....*....|....*
gi 332078559 374 KSLLSGLLIKDPNKR 388
Cdd:cd08228  238 RELVSMCIYPDPDQR 252
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
154-383 6.60e-25

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 103.89  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvaHTLTESRVLKNTRHPFLTSLK------YSFQTKDRLCFVMEY 227
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRE--RWCLEIQIMKRLNHPNVVAARdvpeglQKLAPNDLPLLAMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSR-ERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI---KITDFGLCKEgITDAA 301
Cdd:cd14038   80 CQGGDLRKYLNQfENCcgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKE-LDQGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-----QDHEKLFE-----LILMED----IKFPR 367
Cdd:cd14038  159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPnwqpvQWHGKVRQksnedIVVYEDltgaVKFSS 238
                        250
                 ....*....|....*...
gi 332078559 368 TL--SSDAKSLLSGLLIK 383
Cdd:cd14038  239 VLptPNNLNGILAGKLER 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
146-388 6.65e-25

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: 104.04  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKI--------LKKEViiakdevahtLTESRVLKNTRHPFLTSLKYSF-- 215
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTittdpnpdVQKQI----------LRELEINKSCASPYIVKYYGAFld 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 216 QTKDRLCFVMEYVNGGELffhlsrERVFSEDRTRfyGAEI------------VSALDYLHSGKIVYRDLKLENLMLDKDG 283
Cdd:cd06621   71 EQDSSIGIAMEYCEGGSL------DSIYKKVKKK--GGRIgekvlgkiaesvLKGLSYLHSRKIIHRDIKPSNILLTRKG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 284 HIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL--FELI--- 358
Cdd:cd06621  143 QVKLCDFGVSGELVNSLA--GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLgpIELLsyi 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 332078559 359 -------LMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd06621  221 vnmpnpeLKDEPENGIKWSESFKDFIEKCLEKDGTRR 257
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
148-402 1.45e-24

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: 102.63  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILK---KEVIIAKDEVAhtltesrVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKvkgADQVLVKKEIS-------ILNIARHRNILRLHESFESHEELVMI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML--DKDGHIKITDFGLCKEgITDAA 301
Cdd:cd14104   75 FEFISGVDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQ-LKPGD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLL 377
Cdd:cd14104  154 KFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDFV 233
                        250       260
                 ....*....|....*....|....*
gi 332078559 378 SGLLIKDPNKRLgggpdDAKEIMRH 402
Cdd:cd14104  234 DRLLVKERKSRM-----TAQEALNH 253
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
154-351 1.55e-24

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: 102.15  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAkDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCI-EERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 --FFHLSRERVFSEDRTRFYgAEIVSALDYLHSGK--IVYRDLKLENLMLDKDGHIKITDFGLCK-----EGITDAATMK 304
Cdd:cd13978   80 ksLLEREIQDVPWSLRFRII-HEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRGTE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 332078559 305 TFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDH 351
Cdd:cd13978  159 NLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAIN 207
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
150-405 1.77e-24

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: 102.78  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07871    7 YVKLdkLGEGTYATVFKGRSKLTENLVALK----EIRLEHEEGApcTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGgELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd07871   83 EYLDS-DLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL------MEDI-------------K 364
Cdd:cd07871  162 NEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFrllgtpTEETwpgvtsneefrsyL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 365 FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07871  242 FPQyraqplinhapRLDTDGIDLLSSLLLYETKSRI-----SAEAALRHSYF 288
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
150-405 6.31e-24

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: 100.91  E-value: 6.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDEVAH--TLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07847    3 YEKLskIGEGSYGVVFKCRNRETGQIVA---IKKFVESEDDPVIKkiALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd07847   80 EYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGrLPFY------NQ-------------DHEKLFE--------- 356
Cdd:cd07847  160 YVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTG-QPLWpgksdvDQlylirktlgdlipRHQQIFStnqffkgls 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 357 ------LILMEDiKFPRtLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07847  239 ipepetREPLES-KFPN-ISSPALSFLKGCLQMDPTERL-----SCEELLEHPYF 286
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
147-400 6.33e-24

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: 101.74  E-value: 6.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiaKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd06615    2 DFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEI---KPAIRNQIIrELKVLHECNSPYIVGFYGAFYSDGEISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATmk 304
Cdd:cd06615   79 EHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELIlmedikFPRTLSSDAKsllsglliKD 384
Cdd:cd06615  157 SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPD-AKELEAM------FGRPVSEGEA--------KE 221
                        250
                 ....*....|....*.
gi 332078559 385 PNKRLGGGPDDAKEIM 400
Cdd:cd06615  222 SHRPVSGHPPDSPRPM 237
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
146-405 6.58e-24

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: 100.96  E-value: 6.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKI-LKKEVIIAKDEVAhtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKfLESEDDKMVKKIA--MREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd07846   79 FEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQD-------------------HEKLF--------- 355
Cdd:cd07846  159 DYVATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGE-PLFPGDsdidqlyhiikclgnliprHQELFqknplfagv 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 356 ------ELILMEDiKFPRtLSSDAKSLLSGLLIKDPNKRLGGGpddakEIMRHSFF 405
Cdd:cd07846  238 rlpevkEVEPLER-RYPK-LSGVVIDLAKKCLHIDPDKRPSCS-----ELLHHEFF 286
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
152-388 1.49e-23

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 103.03  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKIL------KKEVIIAKDEVAHTLT----------ESRVLKNTRHPFLTSLkysf 215
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRVSDGEPFAVKVVdmegmsEADKNRAQAEVCCLLNcdffsivkchEDFAKKDPRNPENVLM---- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 216 qtkdrLCFVMEYVNGGELFFHL-SRE---RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:PTZ00283 114 -----IALVLDYANAGDLRQEIkSRAktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCKegiTDAATM-----KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK-F 365
Cdd:PTZ00283 189 FSK---MYAATVsddvgRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDpL 265
                        250       260
                 ....*....|....*....|...
gi 332078559 366 PRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:PTZ00283 266 PPSISPEMQEIVTALLSSDPKRR 288
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
148-443 1.88e-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: 1.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKK---EVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKDRL--- 221
Cdd:cd07877   19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfqSIIHAK----RTYRELRLLKHMKHENVIGLLDVFTPARSLeef 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 --CFVMEYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgitD 299
Cdd:cd07877   95 ndVYLVTHLMGADLN-NIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARH---T 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL------------------- 359
Cdd:cd07877  171 DDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILrlvgtpgaellkkissesa 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 360 ---------MEDIKFPRTL---SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPPFKPQVT 427
Cdd:cd07877  251 rnyiqsltqMPKMNFANVFigaNPLAVDLLEKMLVLDSDKRI-----TAAQALAHAYFA--QYHDPDDEPVADPYDQSFE 323
                        330
                 ....*....|....*..
gi 332078559 428 SetdtRYFD-EEFTAQT 443
Cdd:cd07877  324 S----RDLLiDEWKSLT 336
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
200-404 1.93e-23

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: 98.97  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 200 LKNTRHPFLTSLkYSFQTKD-------RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDL 272
Cdd:cd14012   52 LKKLRHPNLVSY-LAFSIERrgrsdgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 273 KLENLMLDKDGH---IKITDFGLCKE--GITDAATMKTFCGTPeYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14012  131 HAGNVLLDRDAGtgiVKLTDYSLGKTllDMCSRGSLDEFKQTY-WLPPELaQGSKSPTRKTDVWDLGLLFLQMLFGLDVL 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 347 YNQDHEKLFelilmediKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 404
Cdd:cd14012  210 EKYTSPNPV--------LVSLDLSASLQDFLSKCLSLDPKKRPT-----ALELLPHEF 254
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
151-405 2.19e-23

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: 99.93  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLKNTRH--PFLTS--LKY--SFQTKDRLCFV 224
Cdd:cd14210   18 LSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNK----KRFHQQALVEVKILKHLNDndPDDKHniVRYkdSFIFRGHLCIV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEyVNGGELFFHLSRERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH--IKITDFGL-CKEGitd 299
Cdd:cd14210   94 FE-LLSINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSsCFEG--- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 aATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlMEDIKFP------------- 366
Cdd:cd14210  170 -EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACI-MEVLGVPpkslidkasrrkk 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 367 -----------------------RTLS-----SDAK--SLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14210  248 ffdsngkprpttnskgkkrrpgsKSLAqvlkcDDPSflDFLKKCLRWDPSERM-----TPEEALQHPWI 311
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
151-422 2.47e-23

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: 100.41  E-value: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEV---IIAKdevaHTLTESRVLKNTRHPFLTSLKYSF---QTKDRLC-- 222
Cdd:cd07880   20 LKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFqseLFAK----RAYRELRLLKHMKHENVIGLLDVFtpdLSLDRFHdf 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 -FVMEYVnGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTDaA 301
Cdd:cd07880   96 yLVMPFM-GTDLGKLMKHEKL-SEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ--TD-S 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILM--------------EDIK- 364
Cdd:cd07880  171 EMTGYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHlDQLMEIMKVtgtpskefvqklqsEDAKn 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332078559 365 ----FPRTLSSDAKSLLS-----------GLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPPF 422
Cdd:cd07880  251 yvkkLPRFRKKDFRSLLPnanplavnvleKMLVLDAESRI-----TAAEALAHPYFE--EFHDPEDETEAPPY 316
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
154-407 4.77e-23

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: 99.75  E-value: 4.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKK---EVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTK------DRLCFV 224
Cdd:cd07855   13 IGSGAYGVVCSAIDTKSGQKVAIKKIPNafdVVTTAK----RTLRELKILRHFKHDNIIAIRDILRPKvpyadfKDVYVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGgELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd07855   89 LDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TF----CGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM----------EDIKFPRT- 368
Cdd:cd07855  168 YFmteyVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTvlgtpsqaviNAIGADRVr 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 369 --------------------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 407
Cdd:cd07855  248 ryiqnlpnkqpvpwetlypkADQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAK 301
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
144-389 6.82e-23

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: 6.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMND-FDYLKLLGKGTFGKVILVREKASGKYYAMKI--LKKEVIIAKDEV--AHTLTESRVLKNTRHPFLTSLKYSFQ-T 217
Cdd:cd14041    3 TLNDrYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSlD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLDKD---GHIKITDFGL 292
Cdd:cd14041   83 TDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGtacGEIKITDFGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 293 CK------EGITDAATMKT-FCGTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFE---L 357
Cdd:cd14041  163 SKimdddsYNSVDGMELTSqGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQentI 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 332078559 358 ILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd14041  243 LKATEVQFPPKpvVTPEAKAFIRRCLAYRKEDRI 276
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
151-404 7.35e-23

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: 97.67  E-value: 7.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREkASGKYYAmkiLKKEVIIAKDE--VAHTLTESRVLKNTRH-PFLTSLkYSFQ---TKDRLCFV 224
Cdd:cd14131    6 LKQLGKGGSSKVYKVLN-PKKKIYA---LKRVDLEGADEqtLQSYKNEIELLKKLKGsDRIIQL-YDYEvtdEDDYLYMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYvngGEL----FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLdKDGHIKITDFGLCKEGITDA 300
Cdd:cd14131   81 MEC---GEIdlatILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAKAIQNDT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 A--TMKTFCGTPEYLAPEVLEDNDY----------GRAVDWWGLGVVMYEMMCGRLPFY-------------NQDHEklf 355
Cdd:cd14131  157 TsiVRDSQVGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQhitnpiaklqaiiDPNHE--- 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 332078559 356 elilmedIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd14131  234 -------IEFPDIPNPDLIDVMKRCLQRDPKKRP-----SIPELLNHPF 270
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
150-339 8.78e-23

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: 97.66  E-value: 8.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKLLGKGTFGKVILVREK----ASGKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSLK---YSfQTKDRLC 222
Cdd:cd05081    8 YISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHS---GPDQQRDFQREIQILKALHSDFIVKYRgvsYG-PGRRSLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITD 299
Cdd:cd05081   84 LVMEYLPSGCLRDFLQRHRaRLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKllPLDKD 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 332078559 300 AATMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEM 339
Cdd:cd05081  164 YYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYEL 204
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
148-404 1.20e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 97.39  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILkkEVIIAKDEvaHTLTESRVLKN-TRHP-----FLTSLKYSFQTKDRL 221
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKIL--DPIHDIDE--EIEAEYNILKAlSDHPnvvkfYGMYYKKDVKNGDQL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELF----FHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 297
Cdd:cd06638   96 WLVLELCNGGSVTdlvkGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILMEDIKF--PRTL 369
Cdd:cd06638  176 STRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPPTLhqPELW 255
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 370 SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06638  256 SNEFNDFIRKCLTKDYEKR-----PTVSDLLQHVF 285
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
146-357 1.29e-22

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: 97.37  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSE--ENEEVKETtLRELKMLRTLKQENIVELKEAFRRRGKLYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK---EGitDAA 301
Cdd:cd07848   79 FEYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARnlsEG--SNA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 302 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE--KLFEL 357
Cdd:cd07848  157 NYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ-PLFPGESEidQLFTI 213
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
144-377 1.31e-22

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: 97.82  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMND-FDYLKLLGKGTFGKVILVREKASGKYYAMKI--LKKEVIIAKDEV--AHTLTESRVLKNTRHPFLTSLKYSFQ-T 217
Cdd:cd14040    3 TLNErYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSlD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLDKD---GHIKITDFGL 292
Cdd:cd14040   83 TDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 293 CK------EGITDAATMKTFCGTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFE---LI 358
Cdd:cd14040  163 SKimdddsYGVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentIL 242
                        250       260
                 ....*....|....*....|.
gi 332078559 359 LMEDIKFP--RTLSSDAKSLL 377
Cdd:cd14040  243 KATEVQFPvkPVVSNEAKAFI 263
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
148-404 1.39e-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: 97.39  E-value: 1.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTLTESRVLKNTRHPFLTSLKY-SFQTK------DR 220
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHHRNIATYYgAFIKKsppghdDQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd06636   94 LWLVMEFCGAGSVtdLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEDIKFPRTLSSDA 373
Cdd:cd06636  174 TVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPPPKLKSKKW 251
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 374 K----SLLSGLLIKDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06636  252 SkkfiDFIEGCLVKNYLSR-----PSTEQLLKHPF 281
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
144-388 1.40e-22

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: 97.41  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd08229   22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGEL---FFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITD 299
Cdd:cd08229  102 VLELADAGDLsrmIKHFKKQKRLIPEKTVWkYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELI-LMEDIKFP----RTLSSDAK 374
Cdd:cd08229  182 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLYSLCkKIEQCDYPplpsDHYSEELR 260
                        250
                 ....*....|....
gi 332078559 375 SLLSGLLIKDPNKR 388
Cdd:cd08229  261 QLVNMCINPDPEKR 274
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
147-338 1.42e-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: 97.11  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREK-ASGKYYAMKILKKEVIIAKDEVAHTLTES--RVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLEEVSilRELTLDGHDNIVQLIDSWEYHGHLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLS---RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckegitda 300
Cdd:cd14052   81 QTELCENGSLDVFLSelgLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFG--------- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332078559 301 atMKTFCGTP---------EYLAPEVLEDNDYGRAVDWWGLGVVMYE 338
Cdd:cd14052  152 --MATVWPLIrgieregdrEYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
146-405 1.55e-22

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: 96.14  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREK-------ASGKYYAmkiLKKevIIAKDEVAHTLTESRVLKNTR-HPFLTSLKYSFQT 217
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKlhdlydrNKGRLVA---LKH--IYPTSSPSRILNELECLERLGgSNNVSGLITAFRN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGElFFHLSRERVFSEdrTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD-GHIKITDFGLCkEG 296
Cdd:cd14019   76 EDQVVAVLPYIEHDD-FRDFYRKMSLTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFGLA-QR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ITDAATMKTFC-GTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN--QDHEKLFELIlmedikfprTL--S 370
Cdd:cd14019  152 EEDRPEQRAPRaGTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRFPFFFssDDIDALAEIA---------TIfgS 222
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 371 SDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14019  223 DEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
148-404 1.62e-22

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: 97.48  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTK-------DR 220
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKknppgmdDQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd06637   84 LWLVMEFCGAGSVtdLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEDIKFPR----TL 369
Cdd:cd06637  164 TVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPAPRlkskKW 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 370 SSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 404
Cdd:cd06637  242 SKKFQSFIESCLVKNHSQRPS-----TEQLMKHPF 271
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
154-388 2.84e-22

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: 95.58  E-value: 2.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKasGKYYAMKILKKEVIIAKDEVahtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIESESEKKAFEV-----EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLsrervFSEDRTRFYGAEIV--------SALDYLHSGK---IVYRDLKLENLMLDKDGH-IKITDFGLckegITDAA 301
Cdd:cd14058   74 YNVL-----HGKEPKPIYTAAHAmswalqcaKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGT----ACDIS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP---RTLSSDAKSLL 377
Cdd:cd14058  145 THMTNNkGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPpliKNCPKPIESLM 224
                        250
                 ....*....|.
gi 332078559 378 SGLLIKDPNKR 388
Cdd:cd14058  225 TRCWSKDPEKR 235
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
150-405 3.19e-22

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: 96.61  E-value: 3.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07873    4 YIKLdkLGEGTYATVYKGRSKLTDNLVALK----EIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd07873   80 EYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM----------------EDIK---F 365
Cdd:cd07873  160 EVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRilgtpteetwpgilsnEEFKsynY 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 366 PR-----------TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd07873  240 PKyradalhnhapRLDSDGADLLSKLLQFEGRKRIS-----AEEAMKHPYF 285
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
147-388 5.11e-22

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: 95.10  E-value: 5.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKL---LGKGTFGKVilVREKASGKYYAMKILKKE----VIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKD 219
Cdd:cd14147    1 SFQELRLeevIGIGGFGKV--YRGSWRGELVAVKAARQDpdedISVTAESVRQ---EARLFAMLAHPNIIALKAVCLEEP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVFSEDRTRfYGAEIVSALDYLHSGKIV---YRDLKLENLMLDKDGH--------IKIT 288
Cdd:cd14147   76 NLCLVMEYAAGGPLSRALAGRRVPPHVLVN-WAVQIARGMHYLHCEALVpviHRDLKSNNILLLQPIEnddmehktLKIT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKF--P 366
Cdd:cd14147  155 DFGLARE--WHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLpiP 232
                        250       260
                 ....*....|....*....|..
gi 332078559 367 RTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd14147  233 STCPEPFAQLMADCWAQDPHRR 254
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
149-405 5.41e-22

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: 95.56  E-value: 5.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 149 DYLKL--LGKGTFGKVILVREKASGKYYAMKILKKEViiaKDE-VAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd07861    1 DYTKIekIGEGTYGVVYKGRNKKTGQIVAMKKIRLES---EEEgVPSTaIREISLLKELQHPNIVCLEDVLMQENRLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVN-----------GGElffHLSRERVFSedrtrfYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 293
Cdd:cd07861   78 FEFLSmdlkkyldslpKGK---YMDAELVKS------YLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 KE-GI-TDAATMKTFcgTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRlPFYNQDHE--KLFEL--IL------- 359
Cdd:cd07861  149 RAfGIpVRVYTHEVV--TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKK-PLFHGDSEidQLFRIfrILgtptedi 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 360 ------MEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07861  226 wpgvtsLPDYKntFPKwkkgslrtavkNLDEDGLDLLEKMLIYDPAKRI-----SAKKALVHPYF 285
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
150-405 5.88e-22

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: 95.53  E-value: 5.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07844    2 YKKLdkLGEGSYATVYKGRSKLTGQLVALK----EIRLEHEEGApfTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGgELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd07844   78 EYLDT-DLKQYMDDcGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF------YNQDHeKLFELI---------------LMED 362
Cdd:cd07844  157 NEVVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstdvEDQLH-KIFRVLgtpteetwpgvssnpEFKP 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 363 IKFPRT-------------LSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd07844  236 YSFPFYpprplinhaprldRIPHGEELALKFLQYEPKKRIS-----AAEAMKHPYF 286
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
154-340 7.57e-22

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: 95.01  E-value: 7.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-------KEGITDAATMK- 304
Cdd:cd14222   77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekKKPPPDKPTTKk 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 332078559 305 ------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd14222  157 rtlrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
245-405 7.73e-22

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: 94.33  E-value: 7.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 245 EDRTR-FYgaEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL----CKEGITDAATMKTFCgtPEYLAPEVLE 319
Cdd:cd14022   84 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLedayILRGHDDSLSDKHGC--PAYVSPEILN 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 320 DNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAK 397
Cdd:cd14022  160 TSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----TSQ 234

                 ....*...
gi 332078559 398 EIMRHSFF 405
Cdd:cd14022  235 EILDHPWF 242
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
154-348 8.55e-22

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: 8.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVIlvrekaSGKYY---AMKILK-----KEVIIA-KDEVAhtltesrVLKNTRHPFLTsLKYSFQTKDRLCFV 224
Cdd:cd14062    1 IGSGSFGTVY------KGRWHgdvAVKKLNvtdptPSQLQAfKNEVA-------VLRKTRHVNIL-LFMGYMTKPQLAIV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLS-RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLckegitdaATM 303
Cdd:cd14062   67 TQWCEGSSLYKHLHvLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGL--------ATV 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 304 KTFCGTPEYL----------APEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 348
Cdd:cd14062  139 KTRWSGSQQFeqptgsilwmAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSH 196
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
150-405 9.23e-22

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: 94.21  E-value: 9.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL---LGKGTFGKVILVREKASGKYYA------MKILKKEVIIAKDEVahtltesRVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:cd13983    2 YLKFnevLGRGSFKTVYRAFDTEEGIEVAwneiklRKLPKAERQRFKQEI-------EILKSLKHPNIIKFYDSWESKSK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LC--FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLD-KDGHIKITDFGLCKe 295
Cdd:cd13983   75 KEviFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLAT- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFY-----NQDHEKLFELILMEDIKfpRTLS 370
Cdd:cd13983  154 -LLRQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSectnaAQIYKKVTSGIKPESLS--KVKD 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 371 SDAKSLLSgLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd13983  230 PELKDFIE-KCLKPPDERP-----SARELLEHPFF 258
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
147-402 1.03e-21

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: 94.48  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEV---AHTLTESRVLKNTRHPFLTSLKYSFQTKDR--- 220
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVkalAKLDHPNIVRYNGCWDGFDYDPETSSSNSSrsk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 ---LCFVMEYVNGGELFFHLSRERVFSEDRTR----FYgaEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 293
Cdd:cd14047   87 tkcLFIQMEFCEKGTLESWIEKRNGEKLDKVLaleiFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 KEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMmcgrLPFYNQDHEKLFELILMEDIKFPRTLSSDA 373
Cdd:cd14047  165 TS-LKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL----LHVCDSAFEKSKFWTDLRNGILPDIFDKRY 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 374 K---SLLSGLLIKDPNKRlgggpDDAKEIMRH 402
Cdd:cd14047  240 KiekTIIKKMLSKKPEDR-----PNASEILRT 266
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
148-388 1.11e-21

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: 94.67  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSL-----KYSFQTKDRLC 222
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYA---LKKILCHSKEDVKEAMREIENYRLFNHPNILRLldsqiVKEAGGKKEVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERV----FSEDRTRFYGAEIVSALDYLHSGKIV---YRDLKLENLMLDKDGHIKITDFGLCK- 294
Cdd:cd13986   79 LLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSMNp 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 -----EGITDAATMKTFC---GTPEYLAPE---VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDHEK---LFELILM 360
Cdd:cd13986  159 arieiEGRREALALQDWAaehCTMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF-ERIFQKgdsLALAVLS 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 332078559 361 EDIKFPRT--LSSDAKSLLSGLLIKDPNKR 388
Cdd:cd13986  238 GNYSFPDNsrYSEELHQLVKSMLVVNPAER 267
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
151-348 1.17e-21

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: 94.31  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVIlvrekaSGKYY---AMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTsLKYSFQTKDRLCFVMEY 227
Cdd:cd14150    5 LKRIGTGSFGTVF------RGKWHgdvAVKILKVTEPTPEQLQAFK-NEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLS-RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDAATMK 304
Cdd:cd14150   77 CEGSSLYRHLHvTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQVE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332078559 305 TFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 348
Cdd:cd14150  157 QPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMSGTLPYSN 203
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
146-354 1.49e-21

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: 95.12  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIA-KDEVahtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAiRNQI---IRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATm 303
Cdd:cd06650   82 MEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 304 kTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 354
Cdd:cd06650  161 -SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKEL 210
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
238-405 1.96e-21

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: 92.88  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 238 SRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKL---------------ENLmldKDGHIKitdfglckEGITDAAT 302
Cdd:cd13976   77 SRKRLREPEAARLF-RQIASAVAHCHRNGIVLRDLKLrkfvfadeertklrlESL---EDAVIL--------EGEDDSLS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCgtPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGL 380
Cdd:cd13976  145 DKHGC--PAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSL 222
                        170       180
                 ....*....|....*....|....*
gi 332078559 381 LIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd13976  223 LRREPSERL-----TAEDILLHPWL 242
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
154-345 2.03e-21

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: 93.32  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEviiakDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRF-----DEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRFY-GAEIVSALDYLHSGKIVYRDLKLENL---MLDKDGHIKITDFGLCKEgITDAATMK----- 304
Cdd:cd14065   76 EELLKSMDEQLPWSQRVSlAKDIASGMAYLHSKNIIHRDLNSKNClvrEANRGRNAVVADFGLARE-MPDEKTKKpdrkk 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 332078559 305 --TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 345
Cdd:cd14065  155 rlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVP 196
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
147-366 2.38e-21

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: 93.57  E-value: 2.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKL---LGKGTFGKVilVREKASGKYYAMKILKKEviiAKDEVAHTL----TESRVLKNTRHPFLTSLKYSFQTKD 219
Cdd:cd14145    4 DFSELVLeeiIGIGGFGKV--YRAIWIGDEVAVKAARHD---PDEDISQTIenvrQEAKLFAMLKHPNIIALRGVCLKEP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIV---YRDLKLEN-LMLDK-------DGHIKIT 288
Cdd:cd14145   79 NLCLVMEFARGGPLNRVLSGKRI-PPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNiLILEKvengdlsNKILKIT 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 289 DFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP 366
Cdd:cd14145  158 DFGLARE--WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP 233
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
145-346 3.05e-21

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: 92.80  E-value: 3.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKasGKYYAMKILKKEVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd05039    5 KKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAAQ----AFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHL-SRER--VFSEDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 301
Cdd:cd05039   79 TEYMAKGSLVDYLrSRGRavITRKDQLGF-ALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332078559 302 TMKtfcgTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05039  158 GGK----LPiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
148-405 3.66e-21

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: 93.31  E-value: 3.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHT--LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALK----EIHLDAEEGTPStaIREISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-GItdaaT 302
Cdd:cd07836   78 EYMDKDLKKYMDTHgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAfGI----P 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCG---TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE----KLFELILMED------------ 362
Cdd:cd07836  154 VNTFSNevvTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEdqllKIFRIMGTPTestwpgisqlpe 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 363 --IKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07836  234 ykPTFPRyppqdlqqlfpHADPLGIDLLHRLLQLNPELRI-----SAHDALQHPWF 284
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
152-388 4.14e-21

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: 93.06  E-value: 4.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKV---ILVREKASGKYYAMKILKKEVIIAKDeVAHTLTESRVLKNTRHPFLTSL---KYSFQTKDRL---C 222
Cdd:cd05074   15 RMLGKGEFGSVreaQLKSEDGSFQKVAVKMLKADIFSSSD-IEEFLREAACMKEFDHPNVIKLigvSLRSRAKGRLpipM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRT-------RFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd05074   94 VILPFMKHGDLHTFLLMSRIGEEPFTlplqtlvRFM-IDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gITDAATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE-LILMEDIKFPRTLS 370
Cdd:cd05074  173 -IYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNyLIKGNRLKQPPDCL 251
                        250
                 ....*....|....*...
gi 332078559 371 SDAKSLLSGLLIKDPNKR 388
Cdd:cd05074  252 EDVYELMCQCWSPEPKCR 269
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
147-363 4.17e-21

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: 93.02  E-value: 4.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd06619    2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQK--QIMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHlsreRVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAtmKTF 306
Cdd:cd06619   80 FMDGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIA--KTY 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEDI 363
Cdd:cd06619  154 VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYpqIQKNQGSLMPLQLLQCI 212
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
258-406 4.26e-21

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: 93.78  E-value: 4.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 258 ALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK-----EGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWG 331
Cdd:cd07852  119 ALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARslsqlEEDDENPVLTDYVATRWYRAPEILlGSTRYTKGVDMWS 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 332 LGVVMYEMMCGRLPF-----YNQdHEKLFELILM---EDI-------------------------KFPRTlSSDAKSLLS 378
Cdd:cd07852  199 VGCILGEMLLGKPLFpgtstLNQ-LEKIIEVIGRpsaEDIesiqspfaatmleslppsrpksldeLFPKA-SPDALDLLK 276
                        170       180
                 ....*....|....*....|....*...
gi 332078559 379 GLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd07852  277 KLLVFNPNKRL-----TAEEALRHPYVA 299
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
151-388 5.65e-21

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 92.40  E-value: 5.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKIL-----------KKEVIIAKDevahtltesrvLKntRHPFLTSLKYS--FQT 217
Cdd:cd13985    5 TKQLGEGGFSYVYLAHDVNTGRRYALKRMyfndeeqlrvaIKEIEIMKR-----------LC--GHPNIVQYYDSaiLSS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCF--VMEYVnGGELFFHLSRE--RVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd13985   72 EGRKEVllLMEYC-PGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 ---------LCKEGITDAA---TMKTfcgTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFE 356
Cdd:cd13985  151 sattehyplERAEEVNIIEeeiQKNT---TPMYRAPEMIDLYSKkpiGEKADIWALGCLLYKLCFFKLPF--DESSKLAI 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332078559 357 LILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd13985  226 VAGKYSIPEQPRYSPELHDLIRHMLTPDPAER 257
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
146-413 5.76e-21

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: 92.60  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKdeVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESK--FNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGG---ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLckEGITDAA 301
Cdd:cd06622   79 EYMDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGV--SGNLVAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTFCGTPEYLAPE---VLEDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF-ELILMED---IKFPRTLSS 371
Cdd:cd06622  157 LAKTNIGCQSYMAPErikSGGPNQnptYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaQLSAIVDgdpPTLPSGYSD 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 332078559 372 DAKSLLSGLLIKDPNKRlgggPDDAkEIMRHSFFSGVNWQDV 413
Cdd:cd06622  237 DAQDFVAKCLNKIPNRR----PTYA-QLLEHPWLVKYKNADV 273
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
146-405 7.18e-21

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: 92.82  E-value: 7.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHTLT---ESRVLKNTRHPFLTSL------KYSFQ 216
Cdd:cd07865   12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALK----KVLMENEKEGFPITalrEIKILQLLKHENVVNLieicrtKATPY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 217 TKDRLCF--VMEYVNGgELFFHLSRERV-FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 293
Cdd:cd07865   88 NRYKGSIylVFEFCEH-DLAGLLSNKNVkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 K----EGITDAATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEM---------------------MCG----- 342
Cdd:cd07865  167 RafslAKNSQPNRYTNRVVTLWYRPPELlLGERDYGPPIDMWGAGCIMAEMwtrspimqgnteqhqltlisqLCGsitpe 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 343 ------RLPFYNqdheklfELILMEDIKF-------PRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07865  247 vwpgvdKLELFK-------KMELPQGQKRkvkerlkPYVKDPYALDLIDKLLVLDPAKRI-----DADTALNHDFF 310
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
150-339 9.70e-21

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: 92.06  E-value: 9.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKLLGKGTFGKVILVRE----------------KASGKYYAMKILKKEVIIakdevahtltesrvLKNTRHPFLTSLKY 213
Cdd:cd05038    8 FIKQLGEGHFGSVELCRYdplgdntgeqvavkslQPSGEEQHMSDFKREIEI--------------LRTLDHEYIVKYKG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 214 SFQTKDR--LCFVMEYVNGGELFFHLSRERVfSEDRTRF--YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 289
Cdd:cd05038   74 VCESPGRrsLRLIMEYLPSGSLRDYLQRHRD-QIDLKRLllFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 290 FGLCK--EGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 339
Cdd:cd05038  153 FGLAKvlPEDKEYYYVKEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYEL 205
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
154-352 1.69e-20

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: 90.91  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVIlvREKASGKYYAMKILKKEviiakdevAHTLTESRVLKNTRHpfLTSLKY----------SFQTKDRLCF 223
Cdd:cd13979   11 LGSGGFGSVY--KATYKGETVAVKIVRRR--------RKNRASRQSFWAELN--AARLRHenivrvlaaeTGTDFASLGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 V-MEYVNGGEL--FFHLSRERVFSEDRTRfYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG---LCKEGI 297
Cdd:cd13979   79 IiMEYCGNGTLqqLIYEGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsvKLGEGN 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPfYNQDHE 352
Cdd:cd13979  158 EVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELP-YAGLRQ 211
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
152-405 1.72e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.13  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILK-----KEVIIAKDEVAH------TLTESRVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKiieisNDVTKDRQLVGMcgihftTLRELKIMNEIKHENIMGLVDVYVEGDF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGgELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA 300
Cdd:PTZ00024  95 INLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFCG---------TPE-----YLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELI-L 359
Cdd:PTZ00024 174 YSDTLSKDetmqrreemTSKvvtlwYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGK-PLFPGENEidqlgRIFELLgT 252
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 360 MEDIKFPRTL-----------------------SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:PTZ00024 253 PNEDNWPQAKklplyteftprkpkdlktifpnaSDDAIDLLQSLLKLNPLERI-----SAKEALKHEYF 316
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
153-388 1.77e-20

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 90.68  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKE----------VIIAKDEVAhtLTESrVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd14101    7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNrvqqwsklpgVNPVPNEVA--LLQS-VGGGPGHRGVIRLLDWFEIPEGFL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEY-VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKITDFGlckEGITDA 300
Cdd:cd14101   84 LVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFG---SGATLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKT-FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHEklfelILMEDIKFPRTLSSDAKSLLS 378
Cdd:cd14101  161 DSMYTdFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPF-ERDTD-----ILKAKPSFNKRVSNDCRSLIR 234
                        250
                 ....*....|
gi 332078559 379 GLLIKDPNKR 388
Cdd:cd14101  235 SCLAYNPSDR 244
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
153-350 1.89e-20

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: 90.43  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVilVREKASGKYYAMKILK----KEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14148    1 IIGVGGFGKV--YKGLWRGEEVAVKAARqdpdEDIAVTAENVRQ---EARLFWMLQHPNIIALRGVCLNPPHLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRfYGAEIVSALDYLHSGKIV---YRDLKLEN-LMLDK-------DGHIKITDFGLCKEgi 297
Cdd:cd14148   76 RGGALNRALAGKKVPPHVLVN-WAVQIARGMNYLHNEAIVpiiHRDLKSSNiLILEPienddlsGKTLKITDFGLARE-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 350
Cdd:cd14148  153 WHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREID 205
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
154-344 1.97e-20

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 90.64  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHT-LTESRVLKNTRHPFLtsLKY-SFQTKD-RLCFVMEYVNG 230
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMK----ELIRFDEEAQRNfLKEVKVMRSLDHPNV--LKFiGVLYKDkKLNLITEYIPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GEL--FFHlSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK---EGITDAATMK- 304
Cdd:cd14154   75 GTLkdVLK-DMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARlivEERLPSGNMSp 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 305 ----------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRL 344
Cdd:cd14154  154 setlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII-GRV 208
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
153-350 2.55e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 90.48  E-value: 2.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVilVREKASGKYYAMKILKKE----VIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14146    1 IIGVGGFGKV--YRATWKGQEVAVKAARQDpdedIKATAESVRQ---EAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRF---------YGAEIVSALDYLHSGKIV---YRDLKLEN-LMLDKDGH-------IKIT 288
Cdd:cd14146   76 RGGTLNRALAAANAAPGPRRARripphilvnWAVQIARGMLYLHEEAVVpilHRDLKSSNiLLLEKIEHddicnktLKIT 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 289 DFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 350
Cdd:cd14146  156 DFGLARE--WHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGID 215
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
153-388 2.83e-20

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: 90.01  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLT--ESRVLKNTRHPFLTSLKYS--FQTKDRLCFVMEYV 228
Cdd:cd14102    7 VLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVplEIVLLKKVGSGFRGVIKLLdwYERPDGFLIVMERP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 N-GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKITDFG---LCKEGI-TDaat 302
Cdd:cd14102   87 EpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGsgaLLKDTVyTD--- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 mktFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHEklfelILMEDIKFPRTLSSDAKSLLSGLL 381
Cdd:cd14102  164 ---FDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPF-EQDEE-----ILRGRLYFRRRVSPECQQLIKWCL 234

                 ....*..
gi 332078559 382 IKDPNKR 388
Cdd:cd14102  235 SLRPSDR 241
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
238-405 3.63e-20

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: 89.34  E-value: 3.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 238 SRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKitdfgLCKEGITDAATMK-------TFCGTP 310
Cdd:cd14023   77 SCKRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQ-----LRLESLEDTHIMKgeddalsDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd14023  151 AYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSER 230
                        170
                 ....*....|....*..
gi 332078559 389 LgggpdDAKEIMRHSFF 405
Cdd:cd14023  231 L-----TAPEILLHPWF 242
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
146-354 3.72e-20

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: 91.26  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIA-KDEVahtLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAiRNQI---IRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATm 303
Cdd:cd06649   82 MEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 304 kTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 354
Cdd:cd06649  161 -SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
224-346 4.35e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 92.94  E-value: 4.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK----EGITD 299
Cdd:NF033483  85 VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARalssTTMTQ 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 300 AATMktfCGTPEYLAPEVLEdndyGRAV----DWWGLGVVMYEMMCGRLPF 346
Cdd:NF033483 165 TNSV---LGTVHYLSPEQAR----GGTVdarsDIYSLGIVLYEMLTGRPPF 208
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
145-346 4.54e-20

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: 89.27  E-value: 4.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILvrekasGKYYAMKILKKevIIAKDEVAHT-LTESRVLKNTRHPFLTSL-KYSFQTKDRLC 222
Cdd:cd05082    5 MKELKLLQTIGKGEFGDVML------GDYRGNKVAVK--CIKNDATAQAfLAEASVMTQLRHSNLVQLlGVIVEEKGGLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHL-SRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGitdA 300
Cdd:cd05082   77 IVTEYMAKGSLVDYLrSRGRsVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEA---S 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332078559 301 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05082  154 STQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
146-388 5.19e-20

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 90.05  E-value: 5.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKeVIIAKDEVAHTLTESRVLKNtrHPFLTSLKYSFQTKDR----- 220
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDP-ISDVDEEIEAEYNILRSLPN--HPNVVKFYGMFYKADQyvggq 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGG---ELFFHLSR------ERVFSedrTRFYGAEIvsALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd06639   99 LWLVLELCNGGsvtELVKGLLKcgqrldEAMIS---YILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCKEGITDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-LFEL------IL 359
Cdd:cd06639  174 VSAQLTSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKaLFKIprnpppTL 253
                        250       260
                 ....*....|....*....|....*....
gi 332078559 360 MEDIKFPRTLSsdakSLLSGLLIKDPNKR 388
Cdd:cd06639  254 LNPEKWCRGFS----HFISQCLIKDFEKR 278
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
154-346 6.63e-20

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: 90.24  E-value: 6.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahTLTESRVLKNTRHPF---LTSLKYSFQTKDRLcFVMEYVNG 230
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDV--QMREFEVLKKLNHKNivkLFAIEEELTTRHKV-LVMELCPC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLsrervfsEDRTRFYG----------AEIVSALDYLHSGKIVYRDLKLENLM--LDKDGH--IKITDFGLCKEg 296
Cdd:cd13988   78 GSLYTVL-------EEPSNAYGlpeseflivlRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARE- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 297 ITDAATMKTFCGTPEYLAPEVLE--------DNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd13988  150 LEDDEQFVSLYGTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
145-366 6.71e-20

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: 89.55  E-value: 6.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMK-ILKKEVIIAKDEVahtLTESRVLKNTRHPFLTSLKYS--------F 215
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELAREKV---LREVRALAKLDHPGIVRYFNAwlerppegW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 216 QTKDR---LCFVMEYVNGGELFFHLSReRVFSEDRTRFYG----AEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 288
Cdd:cd14048   82 QEKMDevyLYIQMQLCRKENLKDWMNR-RCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEGITDA------------ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcgrLPFYNQdHEKLFE 356
Cdd:cd14048  161 DFGLVTAMDQGEpeqtvltpmpayAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQ-MERIRT 236
                        250
                 ....*....|
gi 332078559 357 LILMEDIKFP 366
Cdd:cd14048  237 LTDVRKLKFP 246
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
151-404 6.84e-20

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: 90.10  E-value: 6.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd06633   26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckeGITDAATMKTFCGTP 310
Cdd:cd06633  106 SASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG----SASIASPANSFVGTP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 311 EYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDikfPRTLSSDA-----KSLLSGLLI 382
Cdd:cd06633  182 YWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQND---SPTLQSNEwtdsfRGFVDYCLQ 258
                        250       260
                 ....*....|....*....|..
gi 332078559 383 KDPNKRLGGGpddakEIMRHSF 404
Cdd:cd06633  259 KIPQERPSSA-----ELLRHDF 275
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
229-402 7.09e-20

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: 88.40  E-value: 7.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL---CK-EGITDAATMK 304
Cdd:cd14024   67 HYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLedsCPlNGDDDSLTDK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCgtPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLI 382
Cdd:cd14024  147 HGC--PAYVGPEILSSrrSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLR 224
                        170       180
                 ....*....|....*....|
gi 332078559 383 KDPNKRLgggpdDAKEIMRH 402
Cdd:cd14024  225 RSPAERL-----KASEILLH 239
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
151-430 7.94e-20

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: 90.35  E-value: 7.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEV---IIAKdevaHTLTESRVLKNTRHPFLTSL------KYSFQTKDRL 221
Cdd:cd07879   20 LKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFqseIFAK----RAYRELTLLKHMQHENVIGLldvftsAVSGDEFQDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYvnggeLFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGitd 299
Cdd:cd07879   96 YLVMPY-----MQTDLQKIMghPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHA--- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------------MEDI-- 363
Cdd:cd07879  168 DAEMTGYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILkvtgvpgpefvqkLEDKaa 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 364 --------KFPR--------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPPFKPQVT 427
Cdd:cd07879  248 ksyikslpKYPRkdfstlfpKASPQAVDLLEKMLELDVDKRL-----TATEALEHPYFD--SFRDADEETEQQPYDDSLE 320

                 ...
gi 332078559 428 SET 430
Cdd:cd07879  321 NEK 323
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
151-405 9.00e-20

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 89.93  E-value: 9.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKeviIAK-DEVAhtLTESRVLKNTRH--PFLTS----LKYSFQTKDRLCF 223
Cdd:cd14134   17 LRLLGEGTFGKVLECWDRKRKRYVAVKIIRN---VEKyREAA--KIEIDVLETLAEkdPNGKShcvqLRDWFDYRGHMCI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEyVNGGELF-FHLS-RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLEN-LMLD------------------KD 282
Cdd:cd14134   92 VFE-LLGPSLYdFLKKnNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENiLLVDsdyvkvynpkkkrqirvpKS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 283 GHIKITDFGlckegitdAATMK-----TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFEL 357
Cdd:cd14134  171 TDIKLIDFG--------SATFDdeyhsSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLF--QTHDNLEHL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 358 ILMEDI--KFPRTLSSDAKS-----------------------------------------------LLSGLLIKDPNKR 388
Cdd:cd14134  241 AMMERIlgPLPKRMIRRAKKgakyfyfyhgrldwpegsssgrsikrvckplkrlmllvdpehrllfdLIRKMLEYDPSKR 320
                        330
                 ....*....|....*..
gi 332078559 389 LgggpdDAKEIMRHSFF 405
Cdd:cd14134  321 I-----TAKEALKHPFF 332
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
150-405 9.13e-20

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: 89.67  E-value: 9.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKL--LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07872    8 YIKLekLGEGTYATVFKGRSKLTENLVALK----EIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKT 305
Cdd:cd07872   84 EYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------------------MEDIKF 365
Cdd:cd07872  164 EVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFrllgtpteetwpgissndeFKNYNF 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 366 PR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07872  244 PKykpqplinhapRLDTEGIELLTKFLQYESKKRI-----SAEEAMKHAYF 289
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
148-404 1.33e-19

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: 88.28  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckegitdAATMK--- 304
Cdd:cd06607   83 CLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG--------SASLVcpa 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 -TFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDikfPRTLSS-----DAKS 375
Cdd:cd06607  155 nSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND---SPTLSSgewsdDFRN 231
                        250       260
                 ....*....|....*....|....*....
gi 332078559 376 LLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd06607  232 FVDSCLQKIPQDRP-----SAEDLLKHPF 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
148-405 1.51e-19

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: 88.04  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVR---AKKK-TSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGgELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML--DKDGHIKITDFGLCKEGITDAatmKT 305
Cdd:cd14108   80 CHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNE---PQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FC--GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSG 379
Cdd:cd14108  156 YCkyGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESmfkdLCREAKGFIIK 235
                        250       260
                 ....*....|....*....|....*.
gi 332078559 380 LLIKDpnkRLgggPDDAKEIMRHSFF 405
Cdd:cd14108  236 VLVSD---RL---RPDAEETLEHPWF 255
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
153-388 1.57e-19

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: 87.72  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEV---AHTLTESRVLKNTRHPFLTSLKYS--FQTKDRLCFVMEY 227
Cdd:cd14100    7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELpngTRVPMEIVLLKKVGSGFRGVIRLLdwFERPDSFVLVLER 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKITDFG---LCKEGI-TDaa 301
Cdd:cd14100   87 PEPVQDLFDFITERgALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGsgaLLKDTVyTD-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 tmktFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHEklfelILMEDIKFPRTLSSDAKSLLSGL 380
Cdd:cd14100  165 ----FDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPF-EHDEE-----IIRGQVFFRQRVSSECQHLIKWC 234

                 ....*...
gi 332078559 381 LIKDPNKR 388
Cdd:cd14100  235 LALRPSDR 242
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
154-358 2.13e-19

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: 87.81  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVIlvrekaSGKYY---AMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTsLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14151   16 IGSGSFGTVY------KGKWHgdvAVKMLNVTAPTPQQLQAFK-NEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHL-SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFC 307
Cdd:cd14151   88 SSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLS 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 308 GTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELI 358
Cdd:cd14151  168 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMV 222
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
180-377 2.55e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 89.67  E-value: 2.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 180 KKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGgELFFHLSRER------VFSEDRTrfyga 253
Cdd:PHA03212 117 CEHVVIKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRniaicdILAIERS----- 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 254 eIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG-LCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGL 332
Cdd:PHA03212 191 -VLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGaACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSA 269
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 333 GVVMYEMMCGRLPFY-------NQDHEKLFELILMEDIKFPRTLSSDAKSLL 377
Cdd:PHA03212 270 GIVLFEMATCHDSLFekdgldgDCDSDRQIKLIIRRSGTHPNEFPIDAQANL 321
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
153-354 2.60e-19

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: 87.67  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVIlvREKASGKYYAMKILKK-----------EVIIAKDEVAHTLT-------ESRVLKNTRHPFLTSLKYS 214
Cdd:cd14000    1 LLGDGGFGSVY--RASYKGEPVAVKIFNKhtssnfanvpaDTMLRHLRATDAMKnfrllrqELTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 215 fqTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIV----SALDYLHSGKIVYRDLKLENLM---LDKDGHI-- 285
Cdd:cd14000   79 --GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIAlqvaDGLRYLHSAMIIYRDLKSHNVLvwtLYPNSAIii 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 286 KITDFGL----CKEGItdaatmKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKL 354
Cdd:cd14000  157 KIADYGIsrqcCRMGA------KGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPM--VGHLKF 222
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
145-340 2.62e-19

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: 87.95  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMK-ILKKEViiAKDEVAHTLTESRVLKNTRHP--------FLTSLKYSF 215
Cdd:cd14049    5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKkILIKKV--TKRDCMKVLREVKVLAGLQHPnivgyhtaWMEHVQLML 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 216 QTKDRLC--FVMEYVNGGELFFhlsRERVFSEDRTRFYGA--------EIVSALDYLHSGKIVYRDLKLENLMLD-KDGH 284
Cdd:cd14049   83 YIQMQLCelSLWDWIVERNKRP---CEEEFKSAPYTPVDVdvttkilqQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIH 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 285 IKITDFGL-CKEGITDAA-----------TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd14049  160 VRIGDFGLaCPDILQDGNdsttmsrlnglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
152-405 2.69e-19

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 87.18  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKdevahtltESRVLKNTRHPFLTSLKYSFQTKDR-LCFVMEYVNG 230
Cdd:cd14109   10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMR--------EVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLAST 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFH--LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDgHIKITDFGLCKEGITDAATMKTFcG 308
Cdd:cd14109   82 IELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRRLLRGKLTTLIY-G 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 309 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKD 384
Cdd:cd14109  160 SPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSplgnISDDARDFIKKLLVYI 239
                        250       260
                 ....*....|....*....|.
gi 332078559 385 PNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14109  240 PESRL-----TVDEALNHPWF 255
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
147-360 3.09e-19

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: 87.12  E-value: 3.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVilVREKASGKYY-AMKILKkEVIIAKDEVAHtltESRVLKNTRHPFLTSLkYSFQTKDR-LCFV 224
Cdd:cd05059    5 ELTFLKELGSGQFGVV--HLGKWRGKIDvAIKMIK-EGSMSEDDFIE---EAKVMMKLSHPKLVQL-YGVCTKQRpIFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEY-VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd05059   78 TEYmANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTS 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 304 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELILM 360
Cdd:cd05059  158 SVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFsEGKMPYERFSNSEVVEHISQ 216
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
154-344 3.35e-19

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 87.32  E-value: 3.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMK----ELIRFDEETQRTfLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LffhlsRERVFSED-------RTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK- 304
Cdd:cd14221   77 L-----RGIIKSMDshypwsqRVSF-AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEg 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 305 -------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRL 344
Cdd:cd14221  151 lrslkkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII-GRV 202
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
143-389 6.05e-19

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: 87.63  E-value: 6.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 143 KTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEV---IIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTK- 218
Cdd:cd07856    7 EITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFstpVLAK----RTYRELKLLKHLRHENIISLSDIFISPl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 DRLCFVMEYVngGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegIT 298
Cdd:cd07856   83 EDIYFVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR--IQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DaATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI----------LMEDI---- 363
Cdd:cd07856  159 D-PQMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIItellgtppddVINTIcsen 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 332078559 364 ------------------KFPrTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd07856  238 tlrfvqslpkrervpfseKFK-NADPDAIDLLEKMLVFDPKKRI 280
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
152-389 6.80e-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: 87.43  E-value: 6.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKK---EVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd07858   11 KPIGRGAYGIVCSAKNSETNEKVAIKKIANafdNRIDAK----RTLREIKLLRHLDHENVIAIKDIMPPPHREAFNDVYI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGgELF---FH--LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd07858   87 VY-ELMdtdLHqiIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDFM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMcGRLP-FYNQDHEKLFELILM-------EDIKF--------- 365
Cdd:cd07858  166 TEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELL-GRKPlFPGKDYVHQLKLITEllgspseEDLGFirnekarry 244
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 332078559 366 ----PRT-----------LSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd07858  245 irslPYTprqsfarlfphANPLAIDLLEKMLVFDPSKRI 283
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
151-346 6.96e-19

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: 86.55  E-value: 6.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd07870    5 LEKLGEGSYATVYKGISRINGQLVALKVISMK---TEEGVPFTaIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd07870   82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVVT 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332078559 310 PEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd07870  162 LWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAF 199
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
147-352 9.11e-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: 85.86  E-value: 9.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVilvrekASGKYY---AMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd14063    1 ELEIKEVIGKGRFGRV------HRGRWHgdvAIKLLNIDYLNEEQLEAFK-EEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFfHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKdGHIKITDFGLCK-EGITDA 300
Cdd:cd14063   74 VTSLCKGRTLY-SLIHERkeKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSlSGLLQP 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 301 ATMKTFCGTPE----YLAPEVL----------EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE 352
Cdd:cd14063  152 GRREDTLVIPNgwlcYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAE 217
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
148-340 9.34e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 87.24  E-value: 9.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKeviiakdevAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQK---------GTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGgELFFHLSRE-RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKtF 306
Cdd:PHA03209 139 YSS-DLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLG-L 216
                        170       180       190
                 ....*....|....*....|....*....|....
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:PHA03209 217 AGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
151-444 1.16e-18

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: 87.03  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKK---EVIIAKdevaHTLTESRVLKNTRHPFLTSLKYSFQTKDRL-----C 222
Cdd:cd07878   20 LTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfqSLIHAR----RTYRELRLLKHMKHENVIGLLDVFTPATSIenfneV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgiTDaAT 302
Cdd:cd07878   96 YLVTNLMGADLN-NIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ--AD-DE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEDIKFPRTLSSD----- 372
Cdd:cd07878  172 MTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYidqlKRIMEVVGTPSPEVLKKISSEharky 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 373 ----------------------AKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPPFKPqvTSET 430
Cdd:cd07878  252 iqslphmpqqdlkkifrganplAIDLLEKMLVLDSDKRI-----SASEALAHPYFS--QYHDPEDEPEAEPYDE--SPEN 322
                        330
                 ....*....|....*.
gi 332078559 431 DTRYFDE--EFTAQTI 444
Cdd:cd07878  323 KERTIEEwkELTYEEV 338
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
146-346 1.28e-18

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: 86.29  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviiAKDEVAHTLT---ESRVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR-----LQEEEGTPFTairEASLLKGLKHANIVLLHDIIHTKETLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAAT 302
Cdd:cd07869   80 LVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 303 MKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd07869  160 YSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
148-404 1.83e-18

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: 85.87  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckeGITDAATMKTFC 307
Cdd:cd06635  107 CLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG----SASIASPANSFV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 308 GTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD-HEKLFELILMEDIKFPRTLSSDA-KSLLSGLLI 382
Cdd:cd06635  183 GTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNESPTLQSNEWSDYfRNFVDSCLQ 262
                        250       260
                 ....*....|....*....|..
gi 332078559 383 KDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06635  263 KIPQDR-----PTSEELLKHMF 279
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
147-406 2.45e-18

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 85.82  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKilKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLK-----YSFQTKDRL 221
Cdd:cd07849    6 RYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK--KISPFEHQTYCLRTLREIKILLRFKHENIIGILdiqrpPTFESFKDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVnggELFFH-LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegITDA 300
Cdd:cd07849   84 YIVQELM---ETDLYkLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR--IADP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 A-----TMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------MEDIK--- 364
Cdd:cd07849  159 EhdhtgFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILgilgtpsQEDLNcii 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 365 ----------------------FPRTlSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd07849  239 slkarnyikslpfkpkvpwnklFPNA-DPKALDLLDKMLTFNPHKRI-----TVEEALAHPYLE 296
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
144-404 3.25e-18

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: 84.73  E-value: 3.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKevIIAKDEVAHTLTESRV-LKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:cd06618   13 DLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRR--SGNKEENKRILMDLDVvLKSHDCPYIVKCYGYFITDSDVF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVngGELFFHLSReRV---FSEDRTRFYGAEIVSALDYL---HSgkIVYRDLKLENLMLDKDGHIKITDFGLCKEG 296
Cdd:cd06618   91 ICMELM--STCLDKLLK-RIqgpIPEDILGKMTVSIVKALHYLkekHG--VIHRDVKPSNILLDESGNVKLCDFGISGRL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ITDAATMKTfCGTPEYLAPEVLEDNDYG----RAvDWWGLGVVMYEMMCGRLPFYNQDHEklFEL---ILMEDIKFP--- 366
Cdd:cd06618  166 VDSKAKTRS-AGCAAYMAPERIDPPDNPkydiRA-DVWSLGISLVELATGQFPYRNCKTE--FEVltkILNEEPPSLppn 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 367 RTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 404
Cdd:cd06618  242 EGFSPDFCSFVDLCLTKDHRYR-----PKYRELLQHPF 274
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
147-405 4.53e-18

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: 84.20  E-value: 4.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEViiAKDEVAHT-LTESRVLKNTRHPFLTSLKYSF--QTKDRLCF 223
Cdd:cd07843    6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEK--EKEGFPITsLREINILLKLQHPNIVTVKEVVvgSNLDKIYM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVnggE-----LFFHLSRErvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd07843   84 VMEYV---EhdlksLMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 DAATMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELILM--EDI------- 363
Cdd:cd07843  159 PLKPYTQLVVTLWYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKK-PLFPGKSEidqlnKIFKLLGTptEKIwpgfsel 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 364 ------------------KFPRTLSSDAK-SLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07843  238 pgakkktftkypynqlrkKFPALSLSDNGfDLLNRLLTYDPAKRI-----SAEDALKHPYF 293
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
145-384 4.83e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 87.10  E-value: 4.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKdEVAHTLTESRVLKNTRHPFLTSLKYSFQTK--DRLC 222
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKER-EKSQLVIEVNVMRELKHKNIVRYIDRFLNKanQKLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  223 FVMEYVNGGELFFHLSR-ERVFSE-------DRTRfygaEIVSALDYLHSGK-------IVYRDLKLENLMLDKD-GHI- 285
Cdd:PTZ00266   91 ILMEFCDAGDLSRNIQKcYKMFGKieehaivDITR----QLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTGiRHIg 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559  286 ---------------KITDFGLCKE-GITDAAtmKTFCGTPEYLAPEVL--EDNDYGRAVDWWGLGVVMYEMMCGRLPFY 347
Cdd:PTZ00266  167 kitaqannlngrpiaKIGDFGLSKNiGIESMA--HSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFH 244
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 332078559  348 NQDHeklFELILMEDIKFPRtLSSDAKSLLSGLLIKD 384
Cdd:PTZ00266  245 KANN---FSQLISELKRGPD-LPIKGKSKELNILIKN 277
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
185-406 4.92e-18

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 84.00  E-value: 4.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 185 IAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQT--KDRLCFVM--EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALD 260
Cdd:cd14031   48 LTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKKCIVLvtELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 261 YLHSGK--IVYRDLKLENLMLD-KDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMY 337
Cdd:cd14031  128 FLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTSFA--KSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCML 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 338 EMMCGRLPFYN-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd14031  205 EMATSEYPYSEcQNAAQIYRKVTsgIKPASFNKVTDPEVKEIIEGCIRQNKSERL-----SIKDLLNHAFFA 271
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
154-407 5.18e-18

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 85.18  E-value: 5.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGg 231
Cdd:cd07853    8 IGYGAFGVVWSVTDPRDGKRVA---LKKMPNVFQNLVSckRVFRELKMLCFFKHDNVLSALDILQPPHIDPFEEIYVVT- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELF---FH--LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-KEGITDAATMKT 305
Cdd:cd07853   84 ELMqsdLHkiIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLArVEEPDESKHMTQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------MEDIKFPR---------- 367
Cdd:cd07853  164 EVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITdllgtpsLEAMRSACegarahilrg 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 368 -----------TLSSD----AKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 407
Cdd:cd07853  244 phkppslpvlyTLSSQatheAVHLLCRMLVFDPDKRI-----SAADALAHPYLDE 293
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
140-340 5.62e-18

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 83.80  E-value: 5.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 140 HKRktmndfdYLKL---LGKGTFGKVILVR----EKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLK 212
Cdd:cd05080    2 HKR-------YLKKirdLGEGHFGKVSLYCydptNDGTGEMVAVKALKADC--GPQHRSGWKQEIDILKTLYHENIVKYK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 213 --YSFQTKDRLCFVMEYVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDF 290
Cdd:cd05080   73 gcCSEQGGKSLQLIMEYVPLGSLRDYLPKHSI-GLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDF 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 291 GLCK---EG-----ITDAATMKTFcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd05080  152 GLAKavpEGheyyrVREDGDSPVF-----WYAPECLKEYKFYYASDVWSFGVTLYELL 204
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
145-405 5.99e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 84.10  E-value: 5.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiAKDE-VAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLC 222
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLE---QEDEgVPSTaIREISLLKEMQHGNIVRLQDVVHSEKRLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGgELFFHLSRERVFSEDRT--RFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-IKITDFGLCKE-GIt 298
Cdd:PLN00009  78 LVFEYLDL-DLKKHMDSSPDFAKNPRliKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARAfGI- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 299 daaTMKTFCG---TPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELI----------- 358
Cdd:PLN00009 156 ---PVRTFTHevvTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQK-PLFPGDSEidelfKIFRILgtpneetwpgv 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 359 -LMEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:PLN00009 232 tSLPDYKsaFPKwppkdlatvvpTLEPAGVDLLSKMLRLDPSKRI-----TARAALEHEYF 287
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
150-339 6.61e-18

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: 83.91  E-value: 6.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKLLGKGTFGKVILVR----EKASGKYYAMKILKKEViiaKDEVAHTLTESRVLKNTRHPFLTSLK---YSfQTKDRLC 222
Cdd:cd14205    8 FLQQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHST---EEHLRDFEREIEILKSLQHDNIVKYKgvcYS-AGRRNLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FVMEYVNGGELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 301
Cdd:cd14205   84 LIMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 332078559 302 --TMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEM 339
Cdd:cd14205  164 yyKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYEL 204
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
154-405 7.69e-18

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: 83.47  E-value: 7.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKkeVIIAKDEVA-HTLTESRVLKNTR---HPFL-------TSLKYSFQTKDRLC 222
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSVR--VQTNEDGLPlSTVREVALLKRLEafdHPNIvrlmdvcATSRTDRETKVTLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FvmEYVNGgELFFHLSRERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL-----CKE 295
Cdd:cd07863   86 F--EHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLariysCQM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GITDAATmktfcgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLPFYNQDHE-----KLFELILM-------EDI 363
Cdd:cd07863  163 ALTPVVV------TLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF-RRKPLFCGNSEadqlgKIFDLIGLppeddwpRDV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 364 KFPRT----------------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07863  236 TLPRGafsprgprpvqsvvpeIEESGAQLLLEMLTFNPHKRI-----SAFRALQHPFF 288
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
154-346 1.12e-17

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: 83.16  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVilvrekASGKYY---AMKILK------KEVIIAKDEVAhtltesrVLKNTRHPFLTsLKYSFQTKDRLCFV 224
Cdd:cd14149   20 IGSGSFGTV------YKGKWHgdvAVKILKvvdptpEQFQAFRNEVA-------VLRKTRHVNIL-LFMGYMTKDNLAIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLS-RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDAA 301
Cdd:cd14149   86 TQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQ 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 332078559 302 TMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14149  166 QVEQPTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPY 213
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
154-340 1.82e-17

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: 82.28  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKA----SGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKySFQTKDR---LCFVME 226
Cdd:cd05079   12 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYK-GICTEDGgngIKLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA--TM 303
Cdd:cd05079   89 FLPSGSLKEYLPRNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyyTV 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332078559 304 KTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd05079  169 KDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
144-414 2.11e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 82.41  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiaKDEVAHTLTESRVLKNTRH-PFLTSLkYSFQTKDRLC 222
Cdd:cd06616    4 TAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVD--EKEQKRLLMDLDVVMRSSDcPYIVKF-YGALFREGDC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 FV-MEYVNGG-ELFF---HLSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEG 296
Cdd:cd06616   81 WIcMELMDISlDKFYkyvYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ITD-AATMKTFCgTPeYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFEL------ILMEDI 363
Cdd:cd06616  161 VDSiAKTRDAGC-RP-YMAPERIDPSAsrdgYDVRSDVWSLGITLYEVATGKFPYpkWNSVFDQLTQVvkgdppILSNSE 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 364 KFprTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSGVNWQDVY 414
Cdd:cd06616  239 ER--EFSPSFVNFVNLCLIKDESKR-----PKYKELLKHPFIKMYEERNVD 282
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
148-350 2.26e-17

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: 82.76  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckeGITDAATMKTFC 307
Cdd:cd06634   97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG----SASIMAPANSFV 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 332078559 308 GTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 350
Cdd:cd06634  173 GTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMN 218
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
196-405 1.05e-16

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 79.66  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 196 ESRVLKNTRHP----FLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHS--GKIVY 269
Cdd:cd14033   50 EVEMLKGLQHPnivrFYDSWKSTVRGHKCIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrcPPILH 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 270 RDLKLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFYN 348
Cdd:cd14033  130 RDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSE 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 349 -QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14033  207 cQNAAQIYRKVTsgIKPDSFYKVKVPELKEIIEGCIRTDKDERF-----TIQDLLEHRFF 261
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
154-346 1.27e-16

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 79.50  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVilVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTS-LKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd14064    1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQfVGACLDDPSQFAIVTQYVSGGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFFHLSRERVFSEDRTRFYGA-EIVSALDYLH--SGKIVYRDLKLENLMLDKDGHIKITDFG----LCKegiTDAATMKT 305
Cdd:cd14064   79 LFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGesrfLQS---LDEDNMTK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 306 FCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14064  156 QPGNLRWMAPEVFTQCtRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
147-346 1.53e-16

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: 79.15  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILvrEKASGKY-YAMKILKkEVIIAKDEVahtLTESRVLKNTRHPFLTSLkYSFQTKDRLCF-V 224
Cdd:cd05113    5 DLTFLKELGTGQFGVVKY--GKWRGQYdVAIKMIK-EGSMSEDEF---IEEAKVMMNLSHEKLVQL-YGVCTKQRPIFiI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSrervfsEDRTRFYGAEIVS-------ALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 297
Cdd:cd05113   78 TEYMANGCLLNYLR------EMRKRFQTQQLLEmckdvceAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 298 TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05113  152 DDEYTSSVGSKFPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
152-388 1.97e-16

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: 79.62  E-value: 1.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVIL-----VREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05045    6 KTLGEGEFGKVVKatafrLKGRAGYTTVAVKMLKENA--SSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGEL--FFHLSR----------------------ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD 282
Cdd:cd05045   84 YAKYGSLrsFLRESRkvgpsylgsdgnrnssyldnpdERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 283 GHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI- 358
Cdd:cd05045  164 RKMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLFNLLk 243
                        250       260       270
                 ....*....|....*....|....*....|...
gi 332078559 359 ---LMEDikfPRTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd05045  244 tgyRMER---PENCSEEMYNLMLTCWKQEPDKR 273
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
254-405 2.49e-16

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: 78.85  E-value: 2.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 254 EIVSALDYLHSGKIVYRDLKLENLMLDKD---GHIK--ITDFGLCKEGITDAATMK---TFCGTPEYLAPEVLEDNDYGR 325
Cdd:cd13982  107 QIASGLAHLHSLNIVHRDLKPQNILISTPnahGNVRamISDFGLCKKLDVGRSSFSrrsGVAGTSGWIAPEMLSGSTKRR 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 326 ---AVDWWGLGVVMYEMMC-GRLPF-------YNQDHEKLFELILMEDIKFPrtlsSDAKSLLSGLLIKDPNKRlgggPd 394
Cdd:cd13982  187 qtrAVDIFSLGCVFYYVLSgGSHPFgdklereANILKGKYSLDKLLSLGEHG----PEAQDLIERMIDFDPEKR----P- 257
                        170
                 ....*....|.
gi 332078559 395 DAKEIMRHSFF 405
Cdd:cd13982  258 SAEEVLNHPFF 268
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
154-358 2.91e-16

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: 78.43  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSCRET--LPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRE--RVFSEDRTRFYGaEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE---GITDAA-TMKTFc 307
Cdd:cd05084   82 LTFLRTEgpRLKVKELIRMVE-NAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREeedGVYAATgGMKQI- 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 308 gTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05084  160 -PVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAV 210
pknD PRK13184
serine/threonine-protein kinase PknD;
145-388 3.38e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.36  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFfHLSRErVFSEDRTRFYGAE-------------IVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:PRK13184  81 MPYIEGYTLK-SLLKS-VWQKESLSKELAEktsvgaflsifhkICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCK-------EGITDAATMKTFC-----------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 353
Cdd:PRK13184 159 AAIfkkleeeDLLDIDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRK 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 332078559 354 lfeLILMEDIKFPRTLS--SDAKSLLSGLLIK----DPNKR 388
Cdd:PRK13184 239 ---ISYRDVILSPIEVApyREIPPFLSQIAMKalavDPAER 276
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
152-388 3.58e-16

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 78.48  E-value: 3.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMK-----------ILKKEVIIAKDevahtltesrvLKNTRH--PFLTSlkYSFQTK 218
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKrvyvndehdlnVCKREIEIMKR-----------LSGHKNivGYIDS--SANRSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 DRLCFV---MEYVNGGELFfHLSRERVfsedRTRFYGAEIVS-------ALDYLHSGK--IVYRDLKLENLMLDKDGHIK 286
Cdd:cd14037   76 NGVYEVlllMEYCKGGGVI-DLMNQRL----QTGLTESEILKifcdvceAVAAMHYLKppLIHRDLKVENVLISDSGNYK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 287 ITDFGLCKEGITDAATMKTFC---------GTPEYLAPEVLedNDYGRAV-----DWWGLGVVMYemmcgRLPFYNQDHE 352
Cdd:cd14037  151 LCDFGSATTKILPPQTKQGVTyveedikkyTTLQYRAPEMI--DLYRGKPiteksDIWALGCLLY-----KLCFYTTPFE 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 332078559 353 KLFEL-ILMEDIKFP--RTLSSDAKSLLSGLLIKDPNKR 388
Cdd:cd14037  224 ESGQLaILNGNFTFPdnSRYSKRLHKLIRYMLEEDPEKR 262
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
152-338 4.21e-16

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: 77.74  E-value: 4.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVI--LVREKASgkyYAMKILKKEviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVN 229
Cdd:cd05085    2 ELLGKGNFGEVYkgTLKDKTP---VAVKTCKED--LPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERvfSEDRTR---FYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE---GITDAATM 303
Cdd:cd05085   77 GGDFLSFLRKKK--DELKTKqlvKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQeddGVYSSSGL 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 332078559 304 KTFcgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 338
Cdd:cd05085  155 KQI--PIKWTAPEALNYGRYSSESDVWSFGILLWE 187
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
148-415 4.24e-16

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: 78.99  E-value: 4.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVA-HTLTESRVLKNTR-HPFLTSLkysfqtkdrlcFVM 225
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAkRALRELKLLRHFRgHKNITCL-----------YDM 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGG---ELFFH-----------LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd07857   71 DIVFPGnfnELYLYeelmeadlhqiIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 LCKeGIT-----DAATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELI------ 358
Cdd:cd07857  151 LAR-GFSenpgeNAGFMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELLGRKPVFKGKDYvDQLNQILqvlgtp 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 359 ---------------------LMEDIKFPRTL---SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVY 414
Cdd:cd07857  230 deetlsrigspkaqnyirslpNIPKKPFESIFpnaNPLALDLLEKLLAFDPTKRI-----SVEEALEHPYLA--IWHDPD 302

                 .
gi 332078559 415 D 415
Cdd:cd07857  303 D 303
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
148-405 5.47e-16

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: 78.48  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKAS--GKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKNGkdGKEYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEVFLEHADKSVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 -----EYVNGGELFFHLSRERVFSEDRT-RFYGAEIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCKe 295
Cdd:cd07842   82 lfdyaEHDLWQIIKFHRQAKRVSIPPSMvKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLAR- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gITDAATMKTFCGTPE-----YLAPEV-LEDNDYGRAVDWWGLGVVMYEM-------------MCGRLPFYNQDHEKLFE 356
Cdd:cd07842  161 -LFNAPLKPLADLDPVvvtiwYRAPELlLGARHYTKAIDIWAIGCIFAELltlepifkgreakIKKSNPFQRDQLERIFE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 357 LI-------------------LMEDIKF--------------PRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHS 403
Cdd:cd07842  240 VLgtptekdwpdikkmpeydtLKSDTKAstypnsllakwmhkHKKPDSQGFDLLRKLLEYDPTKRI-----TAEEALEHP 314

                 ..
gi 332078559 404 FF 405
Cdd:cd07842  315 YF 316
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
155-346 6.90e-16

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: 76.92  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 155 GKGTFGKVILVREKASGKYYAMKILKKeviIAKdevahtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELF 234
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLK---IEK--------EAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 235 FHLSRERvfSE----DRTRFYGAEIVSALDYLHSG---KIVYRDLKLENLMLDKDGHIKITDFGLCKegITDAATMKTFC 307
Cdd:cd14060   71 DYLNSNE--SEemdmDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTTHMSLV 146
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332078559 308 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14060  147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
151-346 7.12e-16

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 77.65  E-value: 7.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 230
Cdd:cd14026    2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHLSRERVFSED----RTRFYgAEIVSALDYLH--SGKIVYRDLKLENLMLDKDGHIKITDFGLCK---EGITDAA 301
Cdd:cd14026   82 GSLNELLHEKDIYPDVawplRLRIL-YEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKwrqLSISQSR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKTF--CGTPEYLAPEVLEDNDYGRAV---DWWGLGVVMYEMMCGRLPF 346
Cdd:cd14026  161 SSKSApeGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPF 210
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
196-406 7.71e-16

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: 77.42  E-value: 7.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 196 ESRVLKNTRHPFLTSLkYSF---QTKDRLCFVM--EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IV 268
Cdd:cd14032   50 EAEMLKGLQHPNIVRF-YDFwesCAKGKRCIVLvtELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppII 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 269 YRDLKLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFY 347
Cdd:cd14032  129 HRDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYS 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 348 N-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd14032  206 EcQNAAQIYRKVTcgIKPASFEKVTDPEIKEIIGECICKNKEERY-----EIKDLLSHAFFA 262
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
151-406 8.35e-16

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: 78.28  E-value: 8.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDEVAHTLTESRVLKNTRHPF--------------LTSLKYSFQ 216
Cdd:cd07854   10 LRPLGCGSNGLVFSAVDSDCDKRVA---VKKIVLTDPQSVKHALREIKIIRRLDHDNivkvyevlgpsgsdLTEDVGSLT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 217 TKDRLCFVMEYVNGgELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI-KITDFGLCKe 295
Cdd:cd07854   87 ELNSVYIVQEYMET-DLANVLEQGPL-SEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLAR- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gITDAA-------TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-KLFELIL------- 359
Cdd:cd07854  164 -IVDPHyshkgylSEGLV--TKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGK-PLFAGAHElEQMQLILesvpvvr 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 360 ---------------MEDIKFPR--------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 406
Cdd:cd07854  240 eedrnellnvipsfvRNDGGEPRrplrdllpGVNPEALDFLEQILTFNPMDRL-----TAEEALMHPYMS 304
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
254-351 9.34e-16

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: 77.15  E-value: 9.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 254 EIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegiTDAATMKTFCGTPEYLAPEVLeDNDYGRAVDWWGLG 333
Cdd:cd13975  110 DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELF-SGKYDNSVDVYAFG 185
                         90       100
                 ....*....|....*....|....*
gi 332078559 334 VVMYEMMCG--RLP-----FYNQDH 351
Cdd:cd13975  186 ILFWYLCAGhvKLPeafeqCASKDH 210
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
152-346 9.84e-16

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 76.84  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVIlvrekaSGKYYAMKILKKevIIAKDEVAHT-LTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYVNG 230
Cdd:cd05083   12 EIIGEGEFGAVL------QGEYMGQKVAVK--NIKCDVTAQAfLEETAVMTKLQHKNLVRL-LGVILHNGLYIVMELMSK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GELFFHL-SRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTfcg 308
Cdd:cd05083   83 GNLVNFLrSRGRaLVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDNSRL--- 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332078559 309 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05083  160 PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
153-393 1.11e-15

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: 76.53  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVilVREKASGKYYAMKILKKeviiakdevaHTLT-----ESRVLKNTRHPFLTSLkYSFQTKDRLcFVMEY 227
Cdd:cd14068    1 LLGDGGFGSV--YRAVYRGEDVAVKIFNK----------HTSFrllrqELVVLSHLHHPSLVAL-LAAGTAPRM-LVMEL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELFfHLSRERVFSEDRTRFY--GAEIVSALDYLHSGKIVYRDLKLENLML-----DKDGHIKITDFGL----CKEG 296
Cdd:cd14068   67 APKGSLD-ALLQQDNASLTRTLQHriALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIaqycCRMG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ItdaatmKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMM-CGRLpfynqdheklfeliLMEDIKFPRTLSSDAk 374
Cdd:cd14068  146 I------KTSEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILtCGER--------------IVEGLKFPNEFDELA- 204
                        250
                 ....*....|....*....
gi 332078559 375 slLSGLLiKDPNKRLGGGP 393
Cdd:cd14068  205 --IQGKL-PDPVKEYGCAP 220
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
148-342 1.19e-15

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 78.25  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVII---AKDEVAHTLTESRVLKNTRHPFLTSLKYsFQTKDRLCFV 224
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFhrqAAEEIRILEHLKKQDKDNTMNVIHMLES-FTFRNHICMT 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEY--VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH--IKITDFGlckEGITDA 300
Cdd:cd14224  146 FELlsMNLYELI-KKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG---SSCYEH 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 301 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 342
Cdd:cd14224  222 QRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG 263
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
145-360 1.39e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 77.74  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLK--NTRHPFLTS----LKYSFQTK 218
Cdd:cd14226   12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNK----KAFLNQAQIEVRLLElmNKHDTENKYyivrLKRHFMFR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 219 DRLCFVMEYV--NGGELFFHlSRERVFSEDRTRFYGAEIVSALDYLHSG--KIVYRDLKLENLML--DKDGHIKITDFG- 291
Cdd:cd14226   88 NHLCLVFELLsyNLYDLLRN-TNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLcnPKRSAIKIIDFGs 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 292 LCKEGitdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHE-----KLFELILM 360
Cdd:cd14226  167 SCQLG----QRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLFSGANEvdqmnKIVEVLGM 235
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
246-389 1.40e-15

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: 77.45  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 246 DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDaATMKTFCGTPEYLAPEVLEDNDYGR 325
Cdd:cd07850  102 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS-FMMTPYVVTRYYRAPEVILGMGYKE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 326 AVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI--------------------------------LMEDIKFP--- 366
Cdd:cd07850  181 NVDIWSVGCIMGEMIRGTVLFPGTDHidqwNKIIEQLgtpsdefmsrlqptvrnyvenrpkyagysfeeLFPDVLFPpds 260
                        170       180
                 ....*....|....*....|....*..
gi 332078559 367 ----RTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd07850  261 eehnKLKASQARDLLSKMLVIDPEKRI 287
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
113-389 1.60e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 78.54  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 113 EEERMNCSptsqidNIGEEEMDASTTHHK--RKTMNDFDYLKLLGKGTFGKVilvrekasgkYYAMKILKKEVIIAKDEV 190
Cdd:PTZ00036  37 EEERSHNN------NAGEDEDEEKMIDNDinRSPNKSYKLGNIIGNGSFGVV----------YEAICIDTSEKVAIKKVL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 191 AHTLTESR---VLKNTRHP---FLTSLKY--SFQTKDRLCF---VMEYV--NGGELFFHLSRE-RVFSEDRTRFYGAEIV 256
Cdd:PTZ00036 101 QDPQYKNRellIMKNLNHIniiFLKDYYYteCFKKNEKNIFlnvVMEFIpqTVHKYMKHYARNnHALPLFLVKLYSYQLC 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 257 SALDYLHSGKIVYRDLKLENLMLDKDGH-IKITDFGLCKEGITDAATMKTFCgTPEYLAPEV-LEDNDYGRAVDWWGLGV 334
Cdd:PTZ00036 181 RALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYIC-SRFYRAPELmLGATNYTTHIDLWSLGC 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 335 VMYEMMCGRLPFYNQDH-EKLFELILM----------------EDIKFPRTLSSDAK------------SLLSGLLIKDP 385
Cdd:PTZ00036 260 IIAEMILGYPIFSGQSSvDQLVRIIQVlgtptedqlkemnpnyADIKFPDVKPKDLKkvfpkgtpddaiNFISQFLKYEP 339

                 ....
gi 332078559 386 NKRL 389
Cdd:PTZ00036 340 LKRL 343
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
246-421 1.65e-15

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: 77.76  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 246 DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDaATMKTFCGTPEYLAPEVLEDNDYGR 325
Cdd:cd07876  123 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTN-FMMTPYVVTRYYRAPEVILGMGYKE 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 326 AVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI----------LMEDIK-----------------FP-------- 366
Cdd:cd07876  202 NVDIWSVGCIMGELVKGSVIFQGTDHidqwNKVIEQLgtpsaefmnrLQPTVRnyvenrpqypgisfeelFPdwifpses 281
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 367 ---RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPP 421
Cdd:cd07876  282 erdKLKTSQARDLLSKMLVIDPDKRI-----SVDEALRHPYIT--VWYDPAEAEAPPP 332
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
147-406 1.66e-15

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: 76.69  E-value: 1.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvaHTLTESRVLKNTRHPFLTSLKYS--FQTKDR-LCf 223
Cdd:cd06617    2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQK--RLLMDLDISMRSVDCPYTVTFYGalFREGDVwIC- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 vMEYVNGGELFFH---LSRERVFSEDRTRFYGAEIVSALDYLHSG-KIVYRDLKLENLMLDKDGHIKITDFGLCKEGITD 299
Cdd:cd06617   79 -MEVMDTSLDKFYkkvYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 -AATMKTfcGTPEYLAPEVL--EDNDYGRAV--DWWGLGVVMYEMMCGRLPFYN--QDHEKLFELILMEDIKFPR-TLSS 371
Cdd:cd06617  158 vAKTIDA--GCKPYMAPERInpELNQKGYDVksDVWSLGITMIELATGRFPYDSwkTPFQQLKQVVEEPSPQLPAeKFSP 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 332078559 372 DAKSLLSGLLIKDPNKRlgggPDDAkEIMRHSFFS 406
Cdd:cd06617  236 EFQDFVNKCLKKNYKER----PNYP-ELLQHPFFE 265
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
152-341 1.91e-15

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: 76.54  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKasGKYYAMKILKkeviiAKDEVA-HTLTESRVLKNTRHP----FLTSLKYSFQTKDRLCFVME 226
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIFS-----SRDEDSwFRETEIYQTVMLRHEnilgFIAADIKSTGSWTQLWLITE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRERVFSEDRTRFyGAEIVSALDYLHS------GK--IVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd14056   74 YHEHGSLYDYLQRNTLDTEEALRL-AYSAASGLAHLHTeivgtqGKpaIAHRDLKSKNILVKRDGTCCIADLGLAVRYDS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 299 DAATMK----TFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEMMC 341
Cdd:cd14056  153 DTNTIDippnPRVGTKRYMAPEVLDDSinpksfESFKMADIYSFGLVLWEIAR 205
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
154-393 2.17e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 76.61  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVRE-KASGKYYAMKilkkEVIIAKDEVA---HTLTESRVLKNTR---HPFLTSL--KYSFQTKDR---L 221
Cdd:cd07862    9 IGEGAYGKVFKARDlKNGGRFVALK----RVRVQTGEEGmplSTIREVAVLRHLEtfeHPNVVRLfdVCTVSRTDRetkL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGgELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITD 299
Cdd:cd07862   85 TLVFEHVDQ-DLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 300 AATMKTFCgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLPFY--NQDHE---KLFELILM-------EDIKFPR 367
Cdd:cd07862  164 MALTSVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF-RRKPLFrgSSDVDqlgKILDVIGLpgeedwpRDVALPR 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 332078559 368 TLSSD----------------AKSLLSGLLIKDPNKRLGGGP 393
Cdd:cd07862  242 QAFHSksaqpiekfvtdidelGKDLLLKCLTFNPAKRISAYS 283
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
154-345 2.23e-15

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: 75.63  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEViiakDEVAhTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV----DQHK-IVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIK---ITDFGLCKE----GITDAATMKT 305
Cdd:cd14156   76 EELLAREELPLSWREKVeLACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREvgemPANDPERKLS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 345
Cdd:cd14156  156 LVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIP 194
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
195-347 2.37e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 77.58  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 195 TESRVLKNTRHPFLTSLKYSFQTKDRLCFVME--------YVNGGElffHLSRERVFSEDRtrfygaEIVSALDYLHSGK 266
Cdd:PHA03207 135 REIDILKTISHRAIINLIHAYRWKSTVCMVMPkykcdlftYVDRSG---PLPLEQAITIQR------RLLEALAYLHGRG 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 267 IVYRDLKLENLMLDKDGHIKITDFG-LCKegiTDAATMKTFC----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 341
Cdd:PHA03207 206 IIHRDVKTENIFLDEPENAVLGDFGaACK---LDAHPDTPQCygwsGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSV 282

                 ....*.
gi 332078559 342 GRLPFY 347
Cdd:PHA03207 283 KNVTLF 288
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
148-405 2.72e-15

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: 75.93  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDE--VAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVA---LKRVRLDDDDEgvPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVN----------GGELFFHLSRERVFsedrtrfygaEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd07839   79 EYCDqdlkkyfdscNGDIDPEIVKSFMF----------QLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 -GItdaaTMKTFCG---TPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFYN----QDH-EKLFELI------- 358
Cdd:cd07839  149 fGI----PVRCYSAevvTLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQlKRIFRLLgtptees 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 359 ------LMEDIKFPR------------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07839  225 wpgvskLPDYKPYPMypattslvnvvpKLNSTGRDLLQNLLVCNPVQRI-----SAEEALQHPYF 284
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
152-346 3.85e-15

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: 75.22  E-value: 3.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKIlKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLkYSFqTKDRLCFVMEYVNGG 231
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKC-PPSLHVDDSERMELLEEAKKMEMAKFRHILPV-YGI-CSEPVGLVMEYMETG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYgAEIVSALDYLHSGK--IVYRDLKLENLMLDKDGHIKITDFGL--CKEGITDA-ATMKTF 306
Cdd:cd14025   79 SLEKLLASEPLPWELRFRII-HETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLakWNGLSHSHdLSRDGL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 307 CGTPEYLAPE-VLEDND-YGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14025  158 RGTIAYLPPErFKEKNRcPDTKHDVYSFAIVIWGILTQKKPF 199
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
144-405 3.88e-15

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: 76.04  E-value: 3.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILK--KEVIIAKdevahtltESRVLKNTR-HPFLTSLKYSFQTKD- 219
Cdd:cd14132   16 SQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKpvKKKKIKR--------EIKILQNLRgGPNIVKLLDVVKDPQs 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 -RLCFVMEYVNG---GELFFHLSRERVfsedrtRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-IKITDFGLC- 293
Cdd:cd14132   88 kTPSLIFEYVNNtdfKTLYPTLTDYDI------RYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLAe 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 -----KEGITDAATMKtfcgtpeYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFY----NQDH----------EK 353
Cdd:cd14132  162 fyhpgQEYNVRVASRY-------YKGPELLVDYqYYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQlvkiakvlgtDD 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 354 LFELILMEDIKFPRTL------------------------SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14132  235 LYAYLDKYGIELPPRLndilgrhskkpwerfvnsenqhlvTPEALDLLDKLLRYDHQERI-----TAKEAMQHPYF 305
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
142-404 3.91e-15

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: 75.99  E-value: 3.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 142 RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHTLT---ESRVLKNTRHPFLTSLK------ 212
Cdd:cd07864    3 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK----KVRLDNEKEGFPITairEIKILRQLNHRSVVNLKeivtdk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 213 ---YSFQtKDRLCF--VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKI 287
Cdd:cd07864   79 qdaLDFK-KDKGAFylVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 288 TDFGLCKEGITDAA---TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG 342
Cdd:cd07864  158 ADFGLARLYNSEESrpyTNKVI--TLWYRPPElLLGEERYGPAIDVWSCGCILGELftkkpifqanqelaqlelisrLCG 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 343 -----------RLPFYNQ-DHEKLFELILMEDIKFprtLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 404
Cdd:cd07864  236 spcpavwpdviKLPYFNTmKPKKQYRRRLREEFSF---IPTPALDLLDHMLTLDPSKRC-----TAEQALNSPW 301
PH pfam00169
PH domain; PH stands for pleckstrin homology.
6-105 3.98e-15

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 71.05  E-value: 3.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559    6 IVKEGWVQKRGEYIK-NWRPRYFLLKtDGSFIGYKEKPQDVDLPyPLNNFSVAKCQLMKTER----PKPNTFIIRCLQWT 80
Cdd:pfam00169   1 VVKEGWLLKKGGGKKkSWKKRYFVLF-DGSLLYYKDDKSGKSKE-PKGSISLSGCEVVEVVAsdspKRKFCFELRTGERT 78
                          90       100
                  ....*....|....*....|....*
gi 332078559   81 TVIERTFHVDTPEEREEWTEAIQAV 105
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSA 103
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
145-359 4.60e-15

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: 75.07  E-value: 4.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKVIL-----VREKASGKYYAMKILKKEVIIakDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKD 219
Cdd:cd05032    5 REKITLIRELGQGSFGMVYEglakgVVKGEPETRVAIKTVNENASM--RERIEFLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLsRERVFSEDRTRFYG-----------AEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 288
Cdd:cd05032   83 PTLVVMELMAKGDLKSYL-RSRRPEAENNPGLGpptlqkfiqmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 289 DFGLCKEGITDAATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL 359
Cdd:cd05032  162 DFGMTRDIYETDYYRKGGKGLlPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLKFVI 235
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
153-358 6.35e-15

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: 74.84  E-value: 6.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVRekASGKYYAMKILKKEVIIAKDEVAHTL-TESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14158   22 KLGEGGFGVVFKGY--INDKNVAVKKLAAMVDISTEDLTKQFeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFfhlsrERVFSEDRTR----------FYGAeiVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 301
Cdd:cd14158  100 SLL-----DRLACLNDTPplswhmrckiAQGT--ANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQ 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 302 TMKT--FCGTPEYLAPEVLEdNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFELI 358
Cdd:cd14158  173 TIMTerIVGTTAYMAPEALR-GEITPKSDIFSFGVVLLEIITGLPPVdENRDPQLLLDIK 231
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
154-346 9.37e-15

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: 73.92  E-value: 9.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKV---ILVREKASGKYYAMKILKKEVIIA-KDEVahtLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYVN 229
Cdd:cd05060    3 LGHGNFGSVrkgVYLMKSGKEVEVAVKTLKQEHEKAgKKEF---LREASVMAQLDHPCIVRL-IGVCKGEPLMLVMELAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd05060   79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATTAG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 332078559 310 --P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05060  159 rwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
154-358 1.11e-14

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: 73.63  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRET--LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRE--RVFSEDRTRFYGaEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE---GI-TDAATMKTFc 307
Cdd:cd05041   81 LTFLRKKgaRLTVKQLLQMCL-DAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedGEyTVSDGLKQI- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 308 gtP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05041  159 --PiKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQI 209
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
185-405 1.16e-14

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: 74.32  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 185 IAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQT--KDRLCFVM--EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALD 260
Cdd:cd14030   63 LSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvKGKKCIVLvtELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQ 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 261 YLHSGK--IVYRDLKLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMY 337
Cdd:cd14030  143 FLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCML 219
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 338 EMMCGRLPFYN-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd14030  220 EMATSEYPYSEcQNAAQIYRRVTsgVKPASFDKVAIPEVKEIIEGCIRQNKDERYA-----IKDLLNHAFF 285
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
154-358 1.30e-14

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: 73.45  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYyAMKILKKEVIIAKDevahTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd05112   12 IGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEED----FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP-E 311
Cdd:cd05112   87 SDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFPvK 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 332078559 312 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05112  167 WSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI 214
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
151-352 1.46e-14

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: 74.59  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKEVII---AKDEVA--HTLTESRVLKNTRHpfLTSLKYSFQTKDRLCFVM 225
Cdd:cd14212    4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYfrqAMLEIAilTLLNTKYDPEDKHH--IVRLLDHFMHHGHLCIVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EY--VNGGELF-------FHLSRERVFSEdrtrfygaEIVSALDYLHSGKIVYRDLKLENLMLDKD--GHIKITDFG-LC 293
Cdd:cd14212   82 ELlgVNLYELLkqnqfrgLSLQLIRKFLQ--------QLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGsAC 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 294 KEGitdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHE 352
Cdd:cd14212  154 FEN----YTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPLFPGNSE 207
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
151-364 2.23e-14

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: 72.88  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKKeviiakDEVAHTLT-ESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd14016    5 VKKIGSGSFGEVYLGIDLKTGEEVAIKIEKK------DSKHPQLEyEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 --NGGELFfhLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIK---ITDFGLCKEGItDAATM 303
Cdd:cd14016   79 gpSLEDLF--NKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKKYR-DPRTG 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 304 --------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF---YNQDHEKLFELILmeDIK 364
Cdd:cd14016  156 khipyregKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWqglKAQSKKEKYEKIG--EKK 225
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
147-370 2.47e-14

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: 72.85  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVILVREKASGKYyAMKILKKEVIIAKDEVAhtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05148    7 EFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQ---KEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC---KEGITDAA 301
Cdd:cd05148   83 LMEKGSLlaFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliKEDVYLSS 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 302 TMKtfcgTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEDIKFPRTLS 370
Cdd:cd05148  163 DKK----IPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQI-TAGYRMPCPAK 228
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
150-358 2.51e-14

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: 72.59  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKLLGKGTFGKVILVREKASGKYyAMKILKKEVIIAKDevahTLTESRVLKNTRHPFLTSLkYSFQTKDR-LCFVMEYV 228
Cdd:cd05114    8 FMKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEED----FIEEAKVMMKLTHPKLVQL-YGVCTQQKpIYIVTEFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 307
Cdd:cd05114   82 ENGCLLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 308 GTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05114  162 KFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMV 214
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
246-424 3.12e-14

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: 73.93  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 246 DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITdAATMKTFCGTPEYLAPEVLEDNDYGR 325
Cdd:cd07875  126 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT-SFMMTPYVVTRYYRAPEVILGMGYKE 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 326 AVDWWGLGVVMYEMMCGRLPFYNQDH-----------------------------------------EKLF-ELILMEDI 363
Cdd:cd07875  205 NVDIWSVGCIMGEMIKGGVLFPGTDHidqwnkvieqlgtpcpefmkklqptvrtyvenrpkyagysfEKLFpDVLFPADS 284
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 364 KFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPPFKP 424
Cdd:cd07875  285 EHNKLKASQARDLLSKMLVIDASKRI-----SVDEALQHPYIN--VWYDPSEAEAPPPKIP 338
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
156-402 3.55e-14

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: 72.35  E-value: 3.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 156 KGTFGKVILVREKASGKYYAMKILKKEVIIAKDevahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFF 235
Cdd:cd13995   14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSD--------VEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 236 HLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIkITDFGLCKEGITDAATMKTFCGTPEYLAP 315
Cdd:cd13995   86 KLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEIYMSP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 316 EVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL---------MEDIkfPRTLSSDAKSLLSGLLIKDPN 386
Cdd:cd13995  165 EVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLyiihkqappLEDI--AQDCSPAMRELLEAALERNPN 242
                        250
                 ....*....|....*.
gi 332078559 387 KRLgggpdDAKEIMRH 402
Cdd:cd13995  243 HRS-----SAAELLKH 253
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
154-346 4.15e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 72.14  E-value: 4.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVReKASGKYYAMKILKKEVIIAKDevaHTL-TESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd14664    1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGD---HGFqAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 L--FFHLSRERVFSEDRTRFYGAEIVSA--LDYLH---SGKIVYRDLKLENLMLDKDGHIKITDFGLCK-EGITDAATMK 304
Cdd:cd14664   77 LgeLLHSRPESQPPLDWETRQRIALGSArgLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKlMDDKDSHVMS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 305 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 346
Cdd:cd14664  157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
154-345 4.29e-14

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: 72.12  E-value: 4.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKkeviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 233
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNT-----LSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 234 FFHLSRERVFS-EDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLML--DKDGHIKIT-DFGLCkEGITDAATMK---TF 306
Cdd:cd14155   76 EQLLDSNEPLSwTVRVKL-ALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVVgDFGLA-EKIPDYSDGKeklAV 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 345
Cdd:cd14155  154 VGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII-ARIQ 191
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
145-346 4.40e-14

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 72.45  E-value: 4.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 145 MNDFDYLKLLGKGTFGKV---ILVREKASGKY-YAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDR 220
Cdd:cd05057    6 ETELEKGKVLGSGAFGTVykgVWIPEGEKVKIpVAIKVLREET--GPKANEEILDEAYVMASVDHPHLVRL-LGICLSSQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHL--SRERVFSEDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 298
Cdd:cd05057   83 VQLITQLMPLGCLLDYVrnHRDNIGSQLLLNW-CVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDV 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 299 DAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05057  162 DEKEYHAEGGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPY 212
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
154-356 6.00e-14

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 72.33  E-value: 6.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVR----EKASGKYYAMKILKKEVIIakdeVAHTLTESRVLKNTRHPFLTSLKYSFQTKDR--------- 220
Cdd:cd05095   13 LGEGQFGEVHLCEaegmEKFMDKDFALEVSENQPVL----VAVKMLRADANKNARNDFLKEIKIMSRLKDPniirllavc 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 -----LCFVMEYVNGGELFFHLSRE------------RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG 283
Cdd:cd05095   89 itddpLCMITEYMENGDLNQFLSRQqpegqlalpsnaLTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNY 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 284 HIKITDFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CGRLPFYNQDHEKLFE 356
Cdd:cd05095  169 TIKIADFGMSRNLYSgDYYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWETLtfCREQPYSQLSDEQVIE 245
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
406-452 7.53e-14

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 66.23  E-value: 7.53e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 332078559   406 SGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKC 452
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSP 47
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
153-339 1.29e-13

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: 70.93  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVIlvREKASGKYYAMKIL---KKEVIIAKDEVAHTLtesrvlkNTRHP----FLTSLKYSFQTKDRLCFVM 225
Cdd:cd13998    2 VIGKGRFGEVW--KASLKNEPVAVKIFssrDKQSWFREKEIYRTP-------MLKHEnilqFIAADERDTALRTELWLVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFyGAEIVSALDYLHS-------GK--IVYRDLKLENLMLDKDGHIKITDFGLC--- 293
Cdd:cd13998   73 AFHPNGSL*DYLSLHTIDWVSLCRL-ALSVARGLAHLHSeipgctqGKpaIAHRDLKSKNILVKNDGTCCIADFGLAvrl 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 294 --KEGITDAATMKTfCGTPEYLAPEVLED-------NDYGRaVDWWGLGVVMYEM 339
Cdd:cd13998  152 spSTGEEDNANNGQ-VGTKRYMAPEVLEGainlrdfESFKR-VDIYAMGLVLWEM 204
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
154-348 1.75e-13

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: 70.23  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVA-HTLTESRVLKntrhpfltsLKYSFQTKDRLCFVMEYVNGGE 232
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMAcAGLTSPRVVP---------LYGAVREGPWVNIFMDLKEGGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 233 LFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG-HIKITDFG----LCKEGITDAA-TMKTF 306
Cdd:cd13991   85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGhaecLDPDGLGKSLfTGDYI 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 307 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP---FYN 348
Cdd:cd13991  165 PGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPwtqYYS 209
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
154-352 1.81e-13

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: 70.22  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGkYYAMKILKK--------EVIIAKDEVAHTLTESRVLKnTRHPFLTSLKYSFqtkdrlcfVM 225
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTgpnciehnEALLEEGKMMNRLRHSRVVK-LLGVILEEGKYSL--------VM 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG---------LCKEG 296
Cdd:cd14027   71 EYMEKGNLMHVLKKVSVPLSVKGRII-LEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTKEE 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 297 ITDAATMKTFC----GTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHE 352
Cdd:cd14027  150 HNEQREVDGTAkknaGTLYYMAPEHLNDVNAkpTEKSDVYSFAIVLWAIFANKEPYENAINE 211
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
151-385 2.24e-13

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: 70.97  E-value: 2.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYYAMKILKkEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV-- 228
Cdd:cd07859    5 QEVIGKGSYGVVCSAIDTHTGEKVAIKKIN-DVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRREFKDIYVvf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 --NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM--- 303
Cdd:cd07859   84 elMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAifw 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGR--LPFYNQDHeklfELILMEDI---KFPRTLSS----D 372
Cdd:cd07859  164 TDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKplFPGKNVVH----QLDLITDLlgtPSPETISRvrneK 239
                        250
                 ....*....|...
gi 332078559 373 AKSLLSGLLIKDP 385
Cdd:cd07859  240 ARRYLSSMRKKQP 252
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
221-389 3.21e-13

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: 70.28  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDK---DGHIKITDFGLCK--- 294
Cdd:cd13977  110 LWFVMEFCDGGDMNEYLLSRRPDRQTNTSFM-LQLSSALAFLHRNQIVHRDLKPDNILISHkrgEPILKVADFGLSKvcs 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 295 ----EGITDAATMKTF----CGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMcGRLPFYNQDHEKLF---------EL 357
Cdd:cd13977  189 gsglNPEEPANVNKHFlssaCGSDFYMAPEVWEGH-YTAKADIFALGIIIWAMV-ERITFRDGETKKELlgtyiqqgkEI 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 358 I-----LMED--------IKFPRTLSSDAKSLLSGLLIKDPNKRL 389
Cdd:cd13977  267 VplgeaLLENpklelqipLKKKKSMNDDMKQLLRDMLAANPQERP 311
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
6-107 3.26e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 65.65  E-value: 3.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559     6 IVKEGWVQKRGE-YIKNWRPRYFLLkTDGSFIGYKEKPQDVDL----PYPLNNFSVAKCqLMKTERPKPNTFIIRCLQWT 80
Cdd:smart00233   1 VIKEGWLYKKSGgGKKSWKKRYFVL-FNSTLLYYKSKKDKKSYkpkgSIDLSGCTVREA-PDPDSSKKPHCFEIKTSDRK 78
                           90       100
                   ....*....|....*....|....*..
gi 332078559    81 TVIertFHVDTPEEREEWTEAIQAVAD 107
Cdd:smart00233  79 TLL---LQAESEEEREKWVEALRKAIA 102
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
148-347 3.36e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 70.44  E-value: 3.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYS-FQTKDRLCFVME 226
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADEFNFVRAYEcFQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNggELFFHLSRERVFSEDRTRFYGA---EIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGlckegiTD 299
Cdd:cd14229   82 MLE--QNLYDFLKQNKFSPLPLKVIRPilqQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFG------SA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 300 AATMKTFCGT----PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFY 347
Cdd:cd14229  154 SHVSKTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLY 204
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
146-347 3.83e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 70.50  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYS-FQTKDRLCFV 224
Cdd:cd14227   15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYEcFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNggELFFHLSRERVFSEDRTRFYG---AEIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCKEgi 297
Cdd:cd14227   95 FEMLE--QNLYDFLKQNKFSPLPLKYIRpilQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASH-- 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFY 347
Cdd:cd14227  171 VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLY 219
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
154-390 5.47e-13

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 69.65  E-value: 5.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGK-YYAMKILKKeviIAKDEVAHTLtESRVLKNTR-----HPFLTSLKYS-FQTKDRLCFVME 226
Cdd:cd14214   21 LGEGTFGKVVECLDHARGKsQVALKIIRN---VGKYREAARL-EINVLKKIKekdkeNKFLCVLMSDwFNFHGHMCIAFE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVngGELFFHLSRERVFSE---DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-------------------KDGH 284
Cdd:cd14214   97 LL--GKNTFEFLKENNFQPyplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynesksceeksvKNTS 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 285 IKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEDI- 363
Cdd:cd14214  175 IRVADFG---SATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF--QTHENREHLVMMEKIl 249
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332078559 364 -KFPRTL---SSDAKSLLSGLLIKDPNKRLG 390
Cdd:cd14214  250 gPIPSHMihrTRKQKYFYKGSLVWDENSSDG 280
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
146-347 5.51e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 70.12  E-value: 5.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYS-FQTKDRLCFV 224
Cdd:cd14228   15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYEcFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNggELFFHLSRERVFSEDRTRFYG---AEIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCKEgi 297
Cdd:cd14228   95 FEMLE--QNLYDFLKQNKFSPLPLKYIRpilQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH-- 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFY 347
Cdd:cd14228  171 VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLY 219
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
148-347 5.80e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 69.78  E-value: 5.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKD---EVAhTLTESRVLKNTRHPFLTSLKYsFQTKDRLCFV 224
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqiEVS-ILSRLSQENADEFNFVRAYEC-FQHKNHTCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNggELFFHLSRERVFSE---DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDG----HIKITDFGlcKEGI 297
Cdd:cd14211   79 FEMLE--QNLYDFLKQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFG--SASH 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 298 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFY 347
Cdd:cd14211  155 VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLY 203
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
152-359 6.05e-13

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: 68.72  E-value: 6.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVI---LVREKASGKYYAMKILKKEvIIAKDEVAHTLTESRVLKNTRHPFLTSL-KYSFQTKDRLCF---- 223
Cdd:cd05035    5 KILGEGEFGSVMeaqLKQDDGSQLKVAVKTMKVD-IHTYSEIEEFLSEAACMKDFDHPNVMRLiGVCFTASDLNKPpspm 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 -VMEYVNGGELFFHLSRERV------FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEg 296
Cdd:cd05035   84 vILPFMKHGDLHSYLLYSRLgglpekLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRK- 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 297 ITDAATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL 359
Cdd:cd05035  163 IYSGDYYRQGRISKmpvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLR 229
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
154-291 6.56e-13

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: 65.54  E-value: 6.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILKkevIIAKDEVAHTLTESRVLKNTRHPFLTSLKY--SFQTKDRLCFVMEYVNGG 231
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGD---DVNNEEGEDLESEMDILRRLKGLELNIPKVlvTEDVDGPNILLMELVKGG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd13968   78 TLIAYTQEEELDEKDVESIM-YQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
148-405 7.06e-13

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: 69.09  E-value: 7.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAmkiLKKEVIIAKDE--VAHTLTESRVLKNTRHPF----LTSLKYSFQT-KDR 220
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVA---LKKTRLEMEEEgvPSTALREVSLLQMLSQSIyivrLLDVEHVEENgKPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGG-ELFFHLSRE---RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD-GHIKITDFGLCKe 295
Cdd:cd07837   80 LYLVFEYLDTDlKKFIDSYGRgphNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLGR- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 gitdAATMKTFCGTPE-----YLAPEV-LEDNDYGRAVDWWGLGVVMYEMMcGRLPFYNQDHE-----KLFELI------ 358
Cdd:cd07837  159 ----AFTIPIKSYTHEivtlwYRAPEVlLGSTHYSTPVDMWSVGCIFAEMS-RKQPLFPGDSElqqllHIFRLLgtpnee 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 359 -------LMEDIKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd07837  234 vwpgvskLRDWHEYPQwkpqdlsravpDLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
PTZ00284 PTZ00284
protein kinase; Provisional
131-361 8.65e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 69.99  E-value: 8.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 131 EEMDASTTHhkrktmndFDYLKLLGKGTFGKVILVREKASGKYYAMKILK---KEVIIAKDEVAHTLTESRVLKNTRHPF 207
Cdd:PTZ00284 122 EDIDVSTQR--------FKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRnvpKYTRDAKIEIQFMEKVRQADPADRFPL 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 208 LTSLKYSFQTKDRLCFVM-EYvnGGELFFHLSRERVFSEDrtrfYGAEIV----SALDYLHSG-KIVYRDLKLENLMLDK 281
Cdd:PTZ00284 194 MKIQRYFQNETGHMCIVMpKY--GPCLLDWIMKHGPFSHR----HLAQIIfqtgVALDYFHTElHLMHTDLKPENILMET 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 282 DG----------------HIKITDFGLCkegiTDAATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 344
Cdd:PTZ00284 268 SDtvvdpvtnralppdpcRVRICDLGGC----CDERHSRTaIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKL 343
                        250
                 ....*....|....*..
gi 332078559 345 PFynQDHEKLFELILME 361
Cdd:PTZ00284 344 LY--DTHDNLEHLHLME 358
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
153-354 1.24e-12

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 67.86  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKV---ILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTS-LKYSFQTKDRLCFVMEYV 228
Cdd:cd05043   13 LLQEGTFGRIfhgILRDEKGKEEEVLVKTVKDHA--SEIQVTMLLQESSLLYGLSHQNLLPiLHVCIEDGEKPMVLYPYM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGEL--FFHLSRE------RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegitDA 300
Cdd:cd05043   91 NWGNLklFLQQCRLseannpQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSR----DL 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 301 ATMKTFC-GTPEY-----LAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKL 354
Cdd:cd05043  167 FPMDYHClGDNENrpikwMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDPFEM 227
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
152-346 1.44e-12

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: 67.83  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKV---ILVREKASGKYYAMKILKKEVIIAKDEvaHTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYV 228
Cdd:cd05056   12 RCIGEGQFGDVyqgVYMSPENEKIAVAVKTCKNCTSPSVRE--KFLQEAYIMRQFDHPHIVKL-IGVITENPVWIVMELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERVFSEDRTR-FYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFC 307
Cdd:cd05056   89 PLGELRSYLQVNKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRY-MEDESYYKASK 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 308 GT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPF 346
Cdd:cd05056  168 GKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMLGVKPF 209
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
243-421 1.59e-12

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: 68.58  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 243 FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITdAATMKTFCGTPEYLAPEVLEDND 322
Cdd:cd07874  116 LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT-SFMMTPYVVTRYYRAPEVILGMG 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 323 YGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI--------------------------------LMEDIKFP 366
Cdd:cd07874  195 YKENVDIWSVGCIMGEMVRHKILFPGRDYidqwNKVIEQLgtpcpefmkklqptvrnyvenrpkyagltfpkLFPDSLFP 274
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 367 ------RTLSSDAKSLLSGLLIKDPNKRLggGPDDAkeiMRHSFFSgvNWQDVYDKKLVPP 421
Cdd:cd07874  275 adsehnKLKASQARDLLSKMLVIDPAKRI--SVDEA---LQHPYIN--VWYDPAEVEAPPP 328
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
151-405 1.63e-12

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: 68.09  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVI--LVREKASGKYYAMKILKKEVIIaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd08216    3 LYEIGKCFKGGGVvhLAKHKPTNTLVAVKKINLESDS-KEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSRERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 306
Cdd:cd08216   82 AYGSCRDLLKTHFPegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 307 CGTPEY-------LAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPF----------------------------YNQ 349
Cdd:cd08216  162 HDFPKSseknlpwLSPEVLQQNllGYNEKSDIYSVGITACELANGVVPFsdmpatqmllekvrgttpqlldcstyplEED 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332078559 350 DHEKLFELILM-------EDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 405
Cdd:cd08216  242 SMSQSEDSSTEhpnnrdtRDIPYQRTFSEAFHQFVELCLQRDPELRPS-----ASQLLAHSFF 299
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
154-356 2.07e-12

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: 67.69  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYY--------------AMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKD 219
Cdd:cd05097   13 LGEGQFGEVHLCEAEGLAEFLgegapefdgqpvlvAVKMLRADV--TKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVFSE------------DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKI 287
Cdd:cd05097   91 PLCMITEYMENGDLNQFLSQREIESTfthannipsvsiANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKI 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332078559 288 TDFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM--MCGRLPFYNQDHEKLFE 356
Cdd:cd05097  171 ADFGMSRNLYSgDYYRIQGRAVLPiRWMAWESILLGKFTTASDVWAFGVTLWEMftLCKEQPYSLLSDEQVIE 243
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
152-389 2.43e-12

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: 67.15  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILkkeviIAKDEVAHT--LTESRVLKNTR-HP----FLTSLKYSFQTKDRLC-- 222
Cdd:cd14036    6 RVIAEGGFAFVYEAQDVGTGKEYALKRL-----LSNEEEKNKaiIQEINFMKKLSgHPnivqFCSAASIGKEESDQGQae 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 223 --FVMEYVNGG--ELFFHLSRERVFSEDRTR--FYgaEIVSALDYLHSGK--IVYRDLKLENLMLDKDGHIKITDFG--- 291
Cdd:cd14036   81 ylLLTELCKGQlvDFVKKVEAPGPFSPDTVLkiFY--QTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGsat 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 292 ------------LCKEGITDAATMKTfcgTPEYLAPEVLE---DNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLfe 356
Cdd:cd14036  159 teahypdyswsaQKRSLVEDEITRNT---TPMYRTPEMIDlysNYPIGEKQDIWALGCILYLLCFRKHPF--EDGAKL-- 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 332078559 357 LILMEDIKFPrtlSSDAK-----SLLSGLLIKDPNKRL 389
Cdd:cd14036  232 RIINAKYTIP---PNDTQytvfhDLIRSTLKVNPEERL 266
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
152-358 2.75e-12

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: 67.35  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGK-------YYAMKILKKEViiAKDEVAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05101   30 KPLGEGCFGQVVMAEAVGIDKdkpkeavTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERV----FSEDRTRFYGA------------EIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKI 287
Cdd:cd05101  108 IVEYASKGNLREYLRARRPpgmeYSYDINRVPEEqmtfkdlvsctyQLARGMEYLASQKCIHRDLAARNVLVTENNVMKI 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 288 TDFGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05101  188 ADFGLARDINNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKLL 261
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
152-358 3.03e-12

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: 66.95  E-value: 3.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVI--LVREKASGKYYAMKILKKeVIIAKDEVAHTLTESRVLKNTRHPFLTSL-KYSFQTKDRLCF----- 223
Cdd:cd05075    6 KTLGEGEFGSVMegQLNQDDSVLKVAVKTMKI-AICTRSEMEDFLSEAVCMKEFDHPNVMRLiGVCLQNTESEGYpspvv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRER-----VFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 297
Cdd:cd05075   85 ILPFMKHGDLHSFLLYSRlgdcpVYLPTQMLVkFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIY 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332078559 298 T-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05075  165 NgDYYRQGRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYL 228
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
154-338 3.06e-12

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: 66.52  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVI--LVREKASGKYYAMKILKKEVIIA--KDEVahtLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYVN 229
Cdd:cd05116    3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNEANDPalKDEL---LREANVMQQLDNPYIVRM-IGICEAESWMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA--TMKTFC 307
Cdd:cd05116   79 LGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENyyKAQTHG 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 332078559 308 GTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYE 338
Cdd:cd05116  159 KWPvKWYAPECMNYYKFSSKSDVWSFGVLMWE 190
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
151-346 3.47e-12

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: 66.60  E-value: 3.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYyAMKILKKEVIiakdEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVM-EYVN 229
Cdd:cd05072   12 VKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM----SVQAFLEEANLMKTLQHDKLVRL-YAVVTKEEPIYIItEYMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRE---RVFSEDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 306
Cdd:cd05072   86 KGSLLDFLKSDeggKVLLPKLIDF-SAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREG 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 307 CGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05072  165 AKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY 206
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
153-356 4.04e-12

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: 66.22  E-value: 4.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 153 LLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd05047    2 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSED----------------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd05047   82 NLLDFLRKSRVLETDpafaianstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332078559 296 giTDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 356
Cdd:cd05047  162 --QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYE 222
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
154-345 4.34e-12

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 66.77  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASgkYYAMKILKKEVIIAKDEVAHT-LTESRVLKNTRHPFLTSLK-YSFQtKDRLCFVMEYVNGG 231
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSELDWSVVKNSfLTEVEKLSRFRHPNIVDLAgYSAQ-QGNYCLIYVYLPNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVF-----SEDRTRFYGAeiVSALDYLH--SGKIVYRDLKLENLMLDKDGHIKITDFGLCK-------EGI 297
Cdd:cd14159   78 SLEDRLHCQVSCpclswSQRLHVLLGT--ARAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGLARfsrrpkqPGM 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 332078559 298 TDA-ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 345
Cdd:cd14159  156 SSTlARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
144-358 5.15e-12

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: 66.24  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 144 TMNDFDYLKLLGKGTFGKV-----ILVREKASGKYYAMKILKKEVIIA-KDEVAHtltESRVLKNTRHPFLTSLKYSFQT 217
Cdd:cd05048    3 PLSAVRFLEELGEGAFGKVykgelLGPSSEESAISVAIKTLKENASPKtQQDFRR---EAELMSDLQHPNIVCLLGVCTK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALD----------------YLHSGKIVYRDLKLENLMLDK 281
Cdd:cd05048   80 EQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDqsdflhiaiqiaagmeYLSSHHYVHRDLAARNCLVGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 282 DGHIKITDFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEdndYGR---AVDWWGLGVVMYEMMC-GRLPFYNQDHEKLF 355
Cdd:cd05048  160 GLTVKISDFGLSRDIYSsDYYRVQSKSLLPvRWMPPEAIL---YGKfttESDVWSFGVVLWEIFSyGLQPYYGYSNQEVI 236

                 ...
gi 332078559 356 ELI 358
Cdd:cd05048  237 EMI 239
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
151-366 5.35e-12

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: 65.95  E-value: 5.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKA---SGKY--YAMKILKKeviiAKDEvaHTLTESR----VLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd05046   10 ITTLGRGEFGEVFLAKAKGieeEGGEtlVLVKALQK----TKDE--NLQSEFRreldMFRKLSHKNVVRLLGLCREAEPH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVS-------ALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL 292
Cdd:cd05046   84 YMILEYTDLGDLkqFLRATKSKDEKLKPPPLSTKQKVAlctqialGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 293 CKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILMEDIKFP 366
Cdd:cd05046  164 SKDVYNSEYYKLRNALIPlRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELP 239
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
152-388 5.36e-12

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 66.11  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVI---LVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSL-----KYSFQTKDRLCF 223
Cdd:cd14204   13 KVLGEGEFGSVMegeLQQPDGTNHKVAVKTMKLDNF-SQREIEEFLSEAACMKDFNHPNVIRLlgvclEVGSQRIPKPMV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVfsEDRTRF--------YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd14204   92 ILPFMKYGDLHSFLLRSRL--GSGPQHvplqtllkFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN-QDHEKLFELILMEDIKFPRTLSS 371
Cdd:cd14204  170 IYSgDYYRQGRIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGvQNHEIYDYLLHGHRLKQPEDCLD 249
                        250
                 ....*....|....*..
gi 332078559 372 DAKSLLSGLLIKDPNKR 388
Cdd:cd14204  250 ELYDIMYSCWRSDPTDR 266
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
148-388 5.98e-12

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: 65.63  E-value: 5.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKAS--GKYYAMKILKkeviiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd14112    5 FSFGSEIFRGRFSVIVKAVDSTTetDAHCAVKIFE-----VSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGgELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD--KDGHIKITDFGLCKEgiTDAATM 303
Cdd:cd14112   80 EKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQK--VSKLGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 304 KTFCGTPEYLAPEVLEDNDYGRA-VDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEDIKF---PRTLSSDAKSLL 377
Cdd:cd14112  157 VPVDGDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSEydDEEETKENVIFVKCRPnliFVEATQEALRFA 236
                        250
                 ....*....|.
gi 332078559 378 SGLLIKDPNKR 388
Cdd:cd14112  237 TWALKKSPTRR 247
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
152-358 6.60e-12

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: 66.14  E-value: 6.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVilVREKASG---------KYYAMKILKKEviiAKD-EVAHTLTESRVLKNT-RHPFLTSLKYSFQTKDR 220
Cdd:cd05099   18 KPLGEGCFGQV--VRAEAYGidksrpdqtVTVAVKMLKDN---ATDkDLADLISEMELMKLIgKHKNIINLLGVCTQEGP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHLSRERV----FSEDRTRFY------------GAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH 284
Cdd:cd05099   93 LYVIVEYAAKGNLREFLRARRPpgpdYTFDITKVPeeqlsfkdlvscAYQVARGMEYLESRRCIHRDLAARNVLVTEDNV 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 285 IKITDFGLCKeGITDAATM-KTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05099  173 MKIADFGLAR-GVHDIDYYkKTSNGrLPvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFKLL 249
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
152-347 8.07e-12

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: 65.19  E-value: 8.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVI---LVREKASGKYYAMKILKKevIIAKDEVAHTLTESRVLKNTRHP-FLTSLKYSFQTKDRLCFVMEY 227
Cdd:cd05058    1 EVIGKGHFGCVYhgtLIDSDGQKIHCAVKSLNR--ITDIEEVEQFLKEGIIMKDFSHPnVLSLLGICLPSEGSPLVVLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGELffhlsreRVFSEDRTRF--------YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITD 299
Cdd:cd05058   79 MKHGDL-------RNFIRSETHNptvkdligFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARD-IYD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332078559 300 ----AATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 347
Cdd:cd05058  151 keyySVHNHTGAKLPvKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPY 203
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
149-346 8.75e-12

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: 65.29  E-value: 8.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 149 DYLKL---LGKGTFGKVILVREKASGKYyAMKILKKEVIiakdEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVM 225
Cdd:cd05067    7 ETLKLverLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM----SPDAFLAEANLMKQLQHQRLVRL-YAVVTQEPIYIIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 303
Cdd:cd05067   81 EYMENGSLvdFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 332078559 304 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05067  161 REGAKFPiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPY 205
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
152-340 8.85e-12

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 65.86  E-value: 8.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKV--ILVREKASGKY--YAMKILKKeviiakDEVAHTLTESRVLK--NTRHP----FLTSLKYSFQTKDRL 221
Cdd:cd14055    1 KLVGKGRFAEVwkAKLKQNASGQYetVAVKIFPY------EEYASWKNEKDIFTdaSLKHEnilqFLTAEERGVGLDRQY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFFHLSReRVFSEDRTRFYGAEIVSALDYLHSGK---------IVYRDLKLENLMLDKDGHIKITDFGL 292
Cdd:cd14055   75 WLITAYHENGSLQDYLTR-HILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADFGL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 293 C-----KEGITDAATMKTfCGTPEYLAPEVLE------DNDYGRAVDWWGLGVVMYEMM 340
Cdd:cd14055  154 AlrldpSLSVDELANSGQ-VGTARYMAPEALEsrvnleDLESFKQIDVYSMALVLWEMA 211
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
158-405 9.16e-12

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: 65.42  E-value: 9.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 158 TFGKVILVREKASGKYYAMKILKKEViiakdevAHtltesrvLKNTRHP-FLTSLKYSFQTKDRLCFVME---------- 226
Cdd:cd14011   28 VFEKKQLEEYSKRDREQILELLKRGV-------KQ-------LTRLRHPrILTVQHPLEESRESLAFATEpvfaslanvl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 --YVNGGELFFHLSRERVFSEDRTrfYGA-EIVSALDYLH-SGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDA 300
Cdd:cd14011   94 geRDNMPSPPPELQDYKLYDVEIK--YGLlQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCisSEQATDQ 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 301 ATMKTFCG---------TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF--------YNQDHEKLFELILMED 362
Cdd:cd14011  172 FPYFREYDpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNkGKPLFdcvnnllsYKKNSNQLRQLSLSLL 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 332078559 363 IKFPRTLSSDAKSLLSglliKDPNKRLgggpdDAKEIMRHSFF 405
Cdd:cd14011  252 EKVPEELRDHVKTLLN----VTPEVRP-----DAEQLSKIPFF 285
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
152-354 1.13e-11

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 65.37  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKV----------ILVREKASGKYYAMKILKKEVIiakdevahtltesrVLKNTRHPFLTSLKYSFQTKDRL 221
Cdd:cd14152    6 ELIGQGRWGKVhrgrwhgevaIRLLEIDGNNQDHLKLFKKEVM--------------NYRQTRHENVVLFMGACMHPPHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYVNGGELFfHLSRERVFSED--RTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDkDGHIKITDFGLCK-EGIT 298
Cdd:cd14152   72 AIITSFCKGRTLY-SFVRDPKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGiSGVV 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 299 DAATMKTFCGTPE----YLAPEVL------EDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 354
Cdd:cd14152  150 QEGRRENELKLPHdwlcYLAPEIVremtpgKDEDclpFSKAADVYAFGTIWYELQARDWPLKNQPAEAL 218
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
152-358 1.25e-11

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: 65.42  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDE-----VAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05098   19 KPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDatekdLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVIV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRER----------------VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 289
Cdd:cd05098   99 EYASKGNLREYLQARRppgmeycynpshnpeeQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIAD 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 290 FGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05098  179 FGLARDIHHIDYYKKTTNGrlPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKLL 250
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
146-354 1.29e-11

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 65.24  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKY-----YAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDR 220
Cdd:cd05050    5 NNIEYVRDIGQGAFGRVFQARAPGLLPYepftmVAVKMLKEEA--SADMQADFQREAALMAEFDHPNIVKLLGVCAVGKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVNGGELFFHL---------------SRERVFSEDRTRF-------YGAEIVSALDYLHSGKIVYRDLKLENLM 278
Cdd:cd05050   83 MCLLFEYMAYGDLNEFLrhrspraqcslshstSSARKCGLNPLPLscteqlcIAKQVAAGMAYLSERKFVHRDLATRNCL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 279 LDKDGHIKITDFGL---------CKEGITDAATMKtfcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN 348
Cdd:cd05050  163 VGENMVVKIADFGLsrniysadyYKASENDAIPIR-------WMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYG 235

                 ....*.
gi 332078559 349 QDHEKL 354
Cdd:cd05050  236 MAHEEV 241
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
154-345 1.60e-11

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: 64.60  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILvREKASG-----KYYAMKILKKEVIIAKDEVAHTL-------------TESRVLKNTRHPFLTSL-KYS 214
Cdd:cd14067    1 LGQGGSGTVIY-RARYQGqpvavKRFHIKKCKKRTDGSADTMLKHLraadamknfsefrQEASMLHSLQHPCIVYLiGIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 215 FQTkdrLCFVMEYVNGGELffhlsrERVFSEDR------------TRFYGAEIVSALDYLHSGKIVYRDLKLENLM---L 279
Cdd:cd14067   80 IHP---LCFALELAPLGSL------NTVLEENHkgssfmplghmlTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 280 DKDGHI--KITDFGLCKEGITDAATMKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 345
Cdd:cd14067  151 DVQEHIniKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRP 216
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
154-389 1.92e-11

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 64.60  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVR-----EKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05092   13 LGEGAFGKVFLAEchnllPEQDKMLVAVKALKEATESARQDFQR---EAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGEL--FF--HLSRERVFSEDRTRFYG-----------AEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 293
Cdd:cd05092   90 RHGDLnrFLrsHGPDAKILDGGEGQAPGqltlgqmlqiaSQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 KEGI-TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILM-EDIKFPRTL 369
Cdd:cd05092  170 RDIYsTDYYRVGGRTMLPiRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQgRELERPRTC 249
                        250       260
                 ....*....|....*....|
gi 332078559 370 SSDAKSLLSGLLIKDPNKRL 389
Cdd:cd05092  250 PPEVYAIMQGCWQREPQQRH 269
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
151-358 1.99e-11

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: 64.75  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVI------LVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05053   17 GKPLGEGAFGQVVkaeavgLDNKPNEVVTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRER-----------VFSEDRTRFYgaEIVS-------ALDYLHSGKIVYRDLKLENLMLDKDGHI 285
Cdd:cd05053   95 VVEYASKGNLREFLRARRppgeeaspddpRVPEEQLTQK--DLVSfayqvarGMEYLASKKCIHRDLAARNVLVTEDNVM 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 286 KITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05053  173 KIADFGLARDIHHIDYYRKTTNGrLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL 248
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
148-352 2.99e-11

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: 64.72  E-value: 2.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVILVREKASGKYYAMKIlkkevIIAKDEVAH-TLTESRVLKNTR-------HPFLTSLKYsFQTKD 219
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKI-----IRNKKRFHHqALVEVKILDALRrkdrdnsHNVIHMKEY-FYFRN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVnGGELFFHLSRE--RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH--IKITDFG-LCK 294
Cdd:cd14225  119 HLCITFELL-GMNLYELIKKNnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGsSCY 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 295 EgitdAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHE 352
Cdd:cd14225  198 E----HQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTG-YPLFPGENE 250
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
247-340 3.20e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 65.10  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 247 RTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGlckegitdaaTMKTF-----------CGTPEYLAP 315
Cdd:PHA03210 268 QTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFG----------TAMPFekereafdygwVGTVATNSP 337
                         90       100
                 ....*....|....*....|....*
gi 332078559 316 EVLEDNDYGRAVDWWGLGVVMYEMM 340
Cdd:PHA03210 338 EILAGDGYCEITDIWSCGLILLDML 362
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
152-358 3.45e-11

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: 64.27  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDE-----VAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05100   18 KPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDatdkdLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERV----FSEDRTRF------------YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 289
Cdd:cd05100   98 EYASKGNLREYLRARRPpgmdYSFDTCKLpeeqltfkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332078559 290 FGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05100  178 FGLARDVHNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL 249
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
152-350 3.46e-11

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: 63.73  E-value: 3.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGK---YYAMKILKkeVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05066   10 KVIGAGEFGEVCSGRLKLPGKreiPVAIKTLK--AGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAATMKT 305
Cdd:cd05066   88 ENGSLDAFLRKhDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDPEAAYTTR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332078559 306 FCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY---NQD 350
Cdd:cd05066  168 GGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWemsNQD 217
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
154-405 3.75e-11

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: 64.13  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVREKASGKYYAMKILK-----KEViiAKDEVahTLTESRVLKNTRHP-------FLTSLKYSFQTKDRL 221
Cdd:cd14136   18 LGWGHFSTVWLCWDLQNKRFVALKVVKsaqhyTEA--ALDEI--KLLKCVREADPKDPgrehvvqLLDDFKHTGPNGTHV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 222 CFVMEYvnGGELFFHLSRervfsedRTRFYG----------AEIVSALDYLHSG-KIVYRDLKLENLMLD-KDGHIKITD 289
Cdd:cd14136   94 CMVFEV--LGPNLLKLIK-------RYNYRGiplplvkkiaRQVLQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIAD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 290 FGlckegitDAA-TMKTFCG---TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM-------------------------- 339
Cdd:cd14136  165 LG-------NACwTDKHFTEdiqTRQYRSPEVILGAGYGTPADIWSTACMAFELatgdylfdphsgedysrdedhlalii 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 340 -MCGRLP------------FYNQDHE----------KLFElILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDA 396
Cdd:cd14136  238 eLLGRIPrsiilsgkysreFFNRKGElrhisklkpwPLED-VLVEKYKWSKEEAKEFASFLLPMLEYDPEKRA-----TA 311

                 ....*....
gi 332078559 397 KEIMRHSFF 405
Cdd:cd14136  312 AQCLQHPWL 320
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
151-339 4.34e-11

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: 63.61  E-value: 4.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVIlvREKASGKYYAMKILKkeviiAKDEvAHTLTESRVLkNT---RHP----FLTSLKYSFQTKDRLCF 223
Cdd:cd14142   10 VECIGKGRYGEVW--RGQWQGESVAVKIFS-----SRDE-KSWFRETEIY-NTvllRHEnilgFIASDMTSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSEDRTRFyGAEIVSALDYLHS------GK--IVYRDLKLENLMLDKDGHIKITDFGLC-- 293
Cdd:cd14142   81 ITHYHENGSLYDYLQRTTLDHQEMLRL-ALSAASGLVHLHTeifgtqGKpaIAHRDLKSKNILVKSNGQCCIADLGLAvt 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 294 ---KEGITDAATmKTFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEM 339
Cdd:cd14142  160 hsqETNQLDVGN-NPRVGTKRYMAPEVLDETintdcfESYKRVDIYAFGLVLWEV 213
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
150-361 4.60e-11

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 63.43  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKLLGKGTFGKVILvrEKASGKYYAMKILKKEVIIAKD--EVAHTLTESRVLKNTRHP-FLTSLKYSFQTKDRLcFVME 226
Cdd:cd14206    1 YLQEIGNGWFGKVIL--GEIFSDYTPAQVVVKELRVSAGplEQRKFISEAQPYRSLQHPnILQCLGLCTETIPFL-LIME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLSRER--------VFSEDRTRF--YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEG 296
Cdd:cd14206   78 FCQLGDLKRYLRAQRkadgmtpdLPTRDLRTLqrMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 297 ITDAATMktfcgTPEYL-------APEVLED-------NDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELILME 361
Cdd:cd14206  158 YKEDYYL-----TPDRLwiplrwvAPELLDElhgnlivVDQSKESNVWSLGVTIWELFeFGAQPYRHLSDEEVLTFVVRE 232
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
152-354 4.91e-11

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 63.10  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14153    6 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDN----EEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDkDGHIKITDFGLCK-EGITDAATMKTFCGT 309
Cdd:cd14153   82 TLYSVVRDAKvVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFTiSGVLQAGRREDKLRI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 310 PE----YLAPEVL-------EDND--YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 354
Cdd:cd14153  161 QSgwlcHLAPEIIrqlspetEEDKlpFSKHSDVFAFGTIWYELHAREWPFKTQPAEAI 218
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
196-358 5.84e-11

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: 63.11  E-value: 5.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 196 ESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSE---------------DRTRFY--GAEIVSA 258
Cdd:cd05090   57 EASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSPHSDvgcssdedgtvksslDHGDFLhiAIQIAAG 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 259 LDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgitdAATMKTFCGTPE------YLAPEVLEDNDYGRAVDWWGL 332
Cdd:cd05090  137 MEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSRE----IYSSDYYRVQNKsllpirWMPPEAIMYGKFSSDSDIWSF 212
                        170       180
                 ....*....|....*....|....*..
gi 332078559 333 GVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05090  213 GVVLWEIFSfGLQPYYGFSNQEVIEMV 239
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
152-339 6.40e-11

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: 62.74  E-value: 6.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGkviLVRE----KASGKYY--AMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVM 225
Cdd:cd05040    1 EKLGDGSFG---VVRRgewtTPSGKVIqvAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRL-YGVVLSSPLMMVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELffhLSRERvfsEDRTRF-------YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE-GI 297
Cdd:cd05040   77 ELAPLGSL---LDRLR---KDQGHFlistlcdYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRAlPQ 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332078559 298 T-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 339
Cdd:cd05040  151 NeDHYVMQEHRKVPfAWCAPESLKTRKFSHASDVWMFGVTLWEM 194
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
152-346 6.87e-11

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: 62.30  E-value: 6.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVIlvrekaSGKY-----YAMKILKKEVIIAKDevahTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 226
Cdd:cd05034    1 KKLGAGQFGEVW------MGVWngttkVAVKTLKPGTMSPEA----FLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHLS--RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC---KEGITDAA 301
Cdd:cd05034   71 LMSKGSLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLArliEDDEYTAR 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332078559 302 TMKTFcgtP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05034  151 EGAKF---PiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPY 194
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
183-338 8.76e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 63.76  E-value: 8.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 183 VIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGgELFFHLS-RERVFSEDRTRFYGAEIVSALDY 261
Cdd:PHA03211 197 VVVKAGWYASSVHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRS-DLYTYLGaRLRPLGLAQVTAVARQLLSAIDY 275
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332078559 262 LHSGKIVYRDLKLENLMLDKDGHIKITDFG-LC-KEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 338
Cdd:PHA03211 276 IHGEGIIHRDIKTENVLVNGPEDICLGDFGaACfARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFE 354
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
132-339 1.23e-10

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: 61.67  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 132 EMDASTTHHKRKtmndfdylklLGKGTFGKVILVREKASGKYYAMKILKKEVIiakdEVAHTLTESRVLKNTRHPFLTSL 211
Cdd:cd05052    2 EIERTDITMKHK----------LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTM----EVEEFLKEAAVMKEIKHPNLVQL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 212 KYSFQTKDRLCFVMEYVNGGELFFHL-SRERVFSEDRTRFYGA-EIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 289
Cdd:cd05052   68 LGVCTREPPFYIITEFMPYGNLLDYLrECNREELNAVVLLYMAtQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVAD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332078559 290 FGLCKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 339
Cdd:cd05052  148 FGLSRLMTGDTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLLWEI 198
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
151-346 1.28e-10

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: 61.65  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYyAMKILKKEVIIAKDevahTLTESRVLKNTRHPFLTSLkYSFQTKDR-LCFVMEYVN 229
Cdd:cd05068   13 LRKLGSGQFGEVWEGLWNNTTPV-AVKTLKPGTMDPED----FLREAQIMKKLRHPKLIQL-YAVCTLEEpIYIITELMK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 230 GGELFFHLSRE-RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK----EGITDAATMK 304
Cdd:cd05068   87 HGSLLEYLQGKgRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARvikvEDEYEAREGA 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332078559 305 TFcgtP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05068  167 KF---PiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPY 207
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
152-388 1.37e-10

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: 61.81  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGK---YYAMKILKkeVIIAKDEVAHTLTESRVLKNTRHPFLTSLKySFQTKDR-LCFVMEY 227
Cdd:cd05065   10 EVIGAGEFGEVCRGRLKLPGKreiFVAIKTLK--SGYTEKQRRDFLSEASIMGQFDHPNIIHLE-GVVTKSRpVMIITEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGEL--FFHLSRERvFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK---EGITDAAT 302
Cdd:cd05065   87 MENGALdsFLRQNDGQ-FTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleDDTSDPTY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 303 MKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEDIKFPRTLssDAKSLLSG 379
Cdd:cd05065  166 TSSLGGKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDVINAI-EQDYRLPPPM--DCPTALHQ 242
                        250
                 ....*....|...
gi 332078559 380 LLI----KDPNKR 388
Cdd:cd05065  243 LMLdcwqKDRNLR 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
192-388 1.43e-10

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: 61.64  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 192 HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYR 270
Cdd:cd13992   42 TILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSsFIKDIVKGMNYLHSSSIGYH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 271 -DLKLENLMLDKDGHIKITDFGLckEGITDAATMKTFCGTPE-----YLAPEVLEDNDYGR----AVDWWGLGVVMYEMM 340
Cdd:cd13992  122 gRLKSSNCLVDSRWVVKLTDFGL--RNLLEEQTNHQLDEDAQhkkllWTAPELLRGSLLEVrgtqKGDVYSFAIILYEIL 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332078559 341 CGRLPFYNQDHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIK-----DPNKR 388
Cdd:cd13992  200 FRSDPFALEREVAIVEKVISGGNKPFRpelAVLLDEFPPRLVLLVKqcwaeNPEKR 255
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
152-388 2.16e-10

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: 61.23  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYY---AMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDR-LCFVMEY 227
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKKEidvAIKTLKSGY--SDKQRLDFLTEASIMGQFDHPNVIRL-EGVVTKSRpVMIVTEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VNGGEL--FFHLSRERVFSEDRTR-FYGaeIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 304
Cdd:cd05033   87 MENGSLdkFLRENDGKFTVTQLVGmLRG--IASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 305 TFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEDIKFPRTLssDAKSLLSGLL 381
Cdd:cd05033  165 TKGGkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAV-EDGYRLPPPM--DCPSALYQLM 241
                        250
                 ....*....|.
gi 332078559 382 I----KDPNKR 388
Cdd:cd05033  242 LdcwqKDRNER 252
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
8-102 2.61e-10

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 57.33  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   8 KEGWVQKRGEYIKNWRPRYFLLKTD------GSFIGYKEKPQDVdlpyplnnFSVAKCQLMKTERP---KPNTFIIrclq 78
Cdd:cd13276    1 KAGWLEKQGEFIKTWRRRWFVLKQGklfwfkEPDVTPYSKPRGV--------IDLSKCLTVKSAEDatnKENAFEL---- 68
                         90       100
                 ....*....|....*....|....*.
gi 332078559  79 wtTVIERTFHV--DTPEEREEWTEAI 102
Cdd:cd13276   69 --STPEETFYFiaDNEKEKEEWIGAI 92
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
146-356 2.74e-10

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: 61.17  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 146 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFV 224
Cdd:cd05088    7 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSED----------------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 288
Cdd:cd05088   87 IEYAPHGNLLDFLRKSRVLETDpafaianstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 289 DFGLCKEgiTDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 356
Cdd:cd05088  167 DFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYE 234
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
154-389 3.12e-10

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: 60.82  E-value: 3.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVR-----EKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05093   13 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELFFHL-------------SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 295
Cdd:cd05093   90 KHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 296 GI-TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILMEDI-KFPRTLSS 371
Cdd:cd05093  170 VYsTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRPRTCPK 249
                        250
                 ....*....|....*...
gi 332078559 372 DAKSLLSGLLIKDPNKRL 389
Cdd:cd05093  250 EVYDLMLGCWQREPHMRL 267
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
150-367 4.28e-10

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: 60.39  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 150 YLKLLGKGTFGKVIL--VREKASGKYYAMKILKKEVIIaKDEVaHTLTESRVLKNTRHP-FLTSLKYSFQTKDRLcFVME 226
Cdd:cd05087    1 YLKEIGHGWFGKVFLgeVNSGLSSTQVVVKELKASASV-QDQM-QFLEEAQPYRALQHTnLLQCLAQCAEVTPYL-LVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 227 YVNGGELFFHL----SRERVFSEDRT-RFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL--CKEGITD 299
Cdd:cd05087   78 FCPLGDLKGYLrscrAAESMAPDPLTlQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLshCKYKEDY 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 300 AATMKTFCGTPEYLAPEVLED-------NDYGRAVDWWGLGVVMYEMM-CGRLPFYN-QDHEKLFELILMEDIKFPR 367
Cdd:cd05087  158 FVTADQLWVPLRWIAPELVDEvhgnllvVDQTKQSNVWSLGVTIWELFeLGNQPYRHySDRQVLTYTVREQQLKLPK 234
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
154-367 5.68e-10

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: 59.91  E-value: 5.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILvREKASGKYYAMKILKK-EVIIAKDEVAHTLTESRVLKNTRHP-FLTSLKYSFQTKDRLcFVMEYVNGG 231
Cdd:cd05042    3 IGNGWFGKVLL-GEIYSGTSVAQVVVKElKASANPKEQDTFLKEGQPYRILQHPnILQCLGQCVEAIPYL-LVMEFCDLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVF----SEDRT-RFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC----KEGITDAAT 302
Cdd:cd05042   81 DLKAYLRSEREHergdSDTRTlQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhsryKEDYIETDD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 303 MKTFcgtP-EYLAPEVL---EDN----DYGRAVDWWGLGVVMYEMM-CGRLPFYN-QDHEKLFELILMEDIKFPR 367
Cdd:cd05042  161 KLWF---PlRWTAPELVtefHDRllvvDQTKYSNIWSLGVTLWELFeNGAQPYSNlSDLDVLAQVVREQDTKLPK 232
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
152-358 8.14e-10

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: 59.60  E-value: 8.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKY---YAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 228
Cdd:cd05063   11 KVIGAGEFGEVFRGILKMPGRKevaVAIKTLKPGY--TEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 229 NGGELffhlsrERVFSEDRTRFYGAEIVSALD-------YLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 301
Cdd:cd05063   89 ENGAL------DKYLRDHDGEFSSYQLVGMLRgiaagmkYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPE 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 302 TMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05063  163 GTYTTSGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAI 223
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
154-366 8.49e-10

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 59.86  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVI-LVREKASGKYYAMKILK-----KEVIIAKDEVAHTLteSRVLKNTRHPFLTSLKYsFQTKDRLCFVMEY 227
Cdd:cd14213   20 LGEGAFGKVVeCIDHKMGGMHVAVKIVKnvdryREAARSEIQVLEHL--NTTDPNSTFRCVQMLEW-FDHHGHVCIVFEL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 228 VngGELFFHLSRERVFSE---DRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-------------------KDGHI 285
Cdd:cd14213   97 L--GLSTYDFIKENSFLPfpiDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVqsdyvvkynpkmkrdertlKNPDI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 286 KITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEDIKF 365
Cdd:cd14213  175 KVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF--QTHDSKEHLAMMERILG 249

                 .
gi 332078559 366 P 366
Cdd:cd14213  250 P 250
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
147-356 1.19e-09

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: 59.24  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKVI--LVREKASGKYYAMKILKKevIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCF 223
Cdd:cd05089    3 DIKFEDVIGEGNFGQVIkaMIKKDGLKMNAAIKMLKE--FASENDHRDFAGELEVLcKLGHHPNIINLLGACENRGYLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 224 VMEYVNGGELFFHLSRERVFSED----------------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKI 287
Cdd:cd05089   81 AIEYAPYGNLLDFLRKSRVLETDpafakehgtastltsqQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332078559 288 TDFGLCKEgiTDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 356
Cdd:cd05089  161 ADFGLSRG--EEVYVKKTMGRLPvRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYE 229
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
152-346 1.31e-09

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: 58.88  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYyAMKILKKEVIiakdEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYVNGG 231
Cdd:cd05073   17 KKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM----SVEAFLAEANVMKTLQHDKLVKL-HAVVTKEPIYIITEFMAKG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRERVFSEDRTRF--YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd05073   91 SLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKF 170
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332078559 310 P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05073  171 PiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY 209
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
154-356 1.43e-09

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 59.18  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVILVR----------------EKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQT 217
Cdd:cd05096   13 LGEGQFGEVHLCEvvnpqdlptlqfpfnvRKGRPLLVAVKILRPDA--NKNARNDFLKEVKILSRLKDPNIIRLLGVCVD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 218 KDRLCFVMEYVNGGELFFHLSRERVfsEDRTR---------------------FYGAEIVSALDYLHSGKIVYRDLKLEN 276
Cdd:cd05096   91 EDPLCMITEYMENGDLNQFLSSHHL--DDKEEngndavppahclpaisyssllHVALQIASGMKYLSSLNFVHRDLATRN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 277 LMLDKDGHIKITDFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYE--MMCGRLPFYNQDHE 352
Cdd:cd05096  169 CLVGENLTIKIADFGMSRNLYAgDYYRIQGRAVLPiRWMAWECILMGKFTTASDVWAFGVTLWEilMLCKEQPYGELTDE 248

                 ....
gi 332078559 353 KLFE 356
Cdd:cd05096  249 QVIE 252
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
239-405 1.46e-09

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 59.05  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 239 RERVFSEDRTRFYG----AEIVSALDYLHSGKIVYRDLKLENLML--DKDG--HIKITDFGLC----------------- 293
Cdd:cd14018  127 RQYLWVNTPSYRLArvmiLQLLEGVDHLVRHGIAHRDLKSDNILLelDFDGcpWLVIADFGCCladdsiglqlpfsswyv 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 294 -KEGitDAATMktfcgtpeylAPEVLEDN-------DYGRAvDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED--I 363
Cdd:cd14018  207 dRGG--NACLM----------APEVSTAVpgpgvviNYSKA-DAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESqlP 273
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 332078559 364 KFPRTLSSDAKSLLSGLLIKDPNKRLggGPDDAKEIMRHSFF 405
Cdd:cd14018  274 ALPSAVPPDVRQVVKDLLQRDPNKRV--SARVAANVLHLSLW 313
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
147-346 1.66e-09

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 58.88  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 147 DFDYLKLLGKGTFGKV-----------------ILVREKASGKYYAMKILKKEVIIAKDEVAHT-------LTESRVLKN 202
Cdd:cd05108    8 EFKKIKVLGSGAFGTVykglwipegekvkipvaIKELREATSPKANKEILDEAYVMASVDNPHVcrllgicLTSTVQLIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 203 TRHPFLTSLKYSFQTKDRLCfvmeyvngGELFFHlsrervfsedrtrfYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD 282
Cdd:cd05108   88 QLMPFGCLLDYVREHKDNIG--------SQYLLN--------------WCVQIAKGMNYLEDRRLVHRDLAARNVLVKTP 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332078559 283 GHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05108  146 QHVKITDFGLAKLLGAEEKEYHAEGGkVPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPY 212
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
151-358 1.95e-09

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 58.54  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVILVREKASGKYyAMKILKKEVIIAKDevahTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYVNG 230
Cdd:cd05070   14 IKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSPES----FLEEAQIMKKLKHDKLVQL-YAVVSEEPIYIVTEYMSK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 231 GEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG 308
Cdd:cd05070   88 GSLldFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAK 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 309 TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 358
Cdd:cd05070  168 FPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 219
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
8-110 2.55e-09

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 54.23  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559   8 KEGWVQKRGEYIKNWRPRYFLLKtDGSFIGYKE------KPQDVdlpYPLNnfsvAKCQLMKTERPKpnTFIIRCLQwtt 81
Cdd:cd13282    1 KAGYLTKLGGKVKTWKRRWFVLK-NGELFYYKSpndvirKPQGQ---IALD----GSCEIARAEGAQ--TFEIVTEK--- 67
                         90       100       110
                 ....*....|....*....|....*....|.
gi 332078559  82 vieRTF--HVDTPEEREEWTEAIQAVADRLQ 110
Cdd:cd13282   68 ---RTYylTADSENDLDEWIRVIQNVLRRQA 95
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
148-366 2.58e-09

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 58.49  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 148 FDYLKLLGKGTFGKVI-LVREKASGKYYAMKILKKeviIAKDEVAHTLtESRVLK--NTRHPFLTSLKYS----FQTKDR 220
Cdd:cd14215   14 YEIVSTLGEGTFGRVVqCIDHRRGGARVALKIIKN---VEKYKEAARL-EINVLEkiNEKDPENKNLCVQmfdwFDYHGH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 221 LCFVMEYVnGGELFFHLSRERVF--SEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD------------------ 280
Cdd:cd14215   90 MCISFELL-GLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlekkrders 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 281 -KDGHIKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELIL 359
Cdd:cd14215  169 vKSTAIRVVDFG---SATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLF--QTHDNREHLAM 243

                 ....*..
gi 332078559 360 MEDIKFP 366
Cdd:cd14215  244 MERILGP 250
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
154-346 2.98e-09

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: 57.65  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 154 LGKGTFGKVI--LVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTkDRLCFVMEYVNGG 231
Cdd:cd05115   12 LGSGNFGCVKkgVYKMRKKQIDVAIKVLKQGN--EKAVRDEMMREAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 EL--FFHLSRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA--TMKTFC 307
Cdd:cd05115   89 PLnkFLSGKKDEITVSNVVELM-HQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSyyKARSAG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 332078559 308 GTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05115  168 KWPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
151-359 3.32e-09

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: 57.67  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 151 LKLLGKGTFGKVI--LVREKASGK---YYAMKILKKEVIIAkdEVAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCfV 224
Cdd:cd05061   11 LRELGQGSFGMVYegNARDIIKGEaetRVAVKTVNESASLR--ERIEFLNEASVMKGfTCHHVVRLLGVVSKGQPTLV-V 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 225 MEYVNGGELFFHLSRERVFSEDRTRF----------YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK 294
Cdd:cd05061   88 MELMAHGDLKSYLRSLRPEAENNPGRppptlqemiqMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTR 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 295 EGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL 359
Cdd:cd05061  168 DIYETDYYRKGGKGlLPvRWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVM 235
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
152-346 3.71e-09

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 57.43  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVI---LVREKASGKY---YAMKILKKEVIIakDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 225
Cdd:cd05044    1 KFLGSGAFGEVFegtAKDILGDGSGetkVAVKTLRKGATD--QEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 226 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVS-ALD------YLHSGKIVYRDLKLEN-LMLDKDGH---IKITDFGLCK 294
Cdd:cd05044   79 ELMEGGDLLSYLRAARPTAFTPPLLTLKDLLSiCVDvakgcvYLEDMHFVHRDLAARNcLVSSKDYRervVKIGDFGLAR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332078559 295 ------------EGITDAATMktfcgtpeylAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 346
Cdd:cd05044  159 diykndyyrkegEGLLPVRWM----------APESLVDGVFTTQSDVWAFGVLMWEILTlGQQPY 213
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
152-356 3.72e-09

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: 57.23  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 152 KLLGKGTFGKVILVREKASGKYyAMKILKKEVIIAKDevahTLTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEYVNGG 231
Cdd:cd14203    1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMSPEA----FLEEAQIMKKLRHDKLVQL-YAVVSEEPIYIVTEFMSKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 232 ELFFHLSRE--RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT 309
Cdd:cd14203   75 SLLDFLKDGegKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKF 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332078559 310 P-EYLAPEVLEdndYGRAV---DWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 356
Cdd:cd14203  155 PiKWTAPEAAL---YGRFTiksDVWSFGILLTELVTkGRVPYPGMNNREVLE 203
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
220-348 4.51e-09

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 57.45  E-value: 4.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 220 RLCFVMEYVNGGELFFHLSRERVFSEDRTRFyGAEIVSALDYLH------SGK--IVYRDLKLENLMLDKDGHIKITDFG 291
Cdd:cd14143   67 QLWLVSDYHEHGSLFDYLNRYTVTVEGMIKL-ALSIASGLAHLHmeivgtQGKpaIAHRDLKSKNILVKKNGTCCIADLG 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332078559 292 L--CKEGITDAATMKT--FCGTPEYLAPEVLED-------NDYGRAvDWWGLGVVMYEMM----CG------RLPFYN 348
Cdd:cd14143  146 LavRHDSATDTIDIAPnhRVGTKRYMAPEVLDDtinmkhfESFKRA-DIYALGLVFWEIArrcsIGgihedyQLPYYD 222
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
196-340 4.53e-09

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: 57.41  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 196 ESRVLKNTRHPFLTSLKYSFQTKD-RLCFVMEYvnGGELFFHLSRERvFSEDRTRFYGAEIV-------SALDYLHS-GK 266
Cdd:cd14001   55 EAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEY--GGKSLNDLIEER-YEAGLGPFPAATILkvalsiaRALEYLHNeKK 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332078559 267 IVYRDLKLENLMLDKDGH-IKITDFG----LCKEGITDAATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMM 340
Cdd:cd14001  132 ILHGDIKSGNVLIKGDFEsVKLCDFGvslpLTENLEVDSDPKAQYVGTEPWKAKEALEEGgVITDKADIFAYGLVLWEMM 211
 
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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