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Conserved domains on  [gi|42544153|ref|NP_002335|]
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leukocyte tyrosine kinase receptor isoform 1 precursor [Homo sapiens]

Protein Classification

ALK/LTK family receptor protein-tyrosine kinase( domain architecture ID 10141990)

ALK/LTK family receptor protein-tyrosine kinase (RTK) similar to Anaplastic Lymphoma Kinase (ALK) and Leukocyte Tyrosine Kinase (LTK), which are orphan RTKs that contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyrosine (tyr) kinase domain that catalyzes the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
503-779 0e+00

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


:

Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 605.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 503 TEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05036   1 KEVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKI 662
Cdd:cd05036  81 RLPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05036 161 GDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRM 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQY 779
Cdd:cd05036 241 DPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
 
Name Accession Description Interval E-value
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
503-779 0e+00

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 605.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 503 TEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05036   1 KEVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKI 662
Cdd:cd05036  81 RLPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05036 161 GDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRM 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQY 779
Cdd:cd05036 241 DPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
510-777 2.57e-126

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: 379.92  E-value: 2.57e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   510 VTLLRALGHGAFGEVYEGLVIGlPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKG-EGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   590 LELMSGGDMKSFLRHSRPHLGQPsplvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMAR 669
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLK------DLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE---NLVVKISDFGLSR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   670 DIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCP 749
Cdd:pfam07714 151 DIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCP 230
                         250       260
                  ....*....|....*....|....*...
gi 42544153   750 GPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:pfam07714 231 DELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
510-777 2.45e-119

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 361.85  E-value: 2.45e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    510 VTLLRALGHGAFGEVYEGLVIGLPGDSsPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKK-KVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    590 LELMSGGDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMAR 669
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLS------LSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    670 DIYRASYYR-RGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGC 748
Cdd:smart00219 151 DLYDDDYYRkRGGK--LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNC 228
                          250       260
                   ....*....|....*....|....*....
gi 42544153    749 PGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:smart00219 229 PPELYDLMLQCWAEDPEDRPTFSELVEIL 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
511-847 4.77e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 125.13  E-value: 4.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGLPgdsspLQVAIKTL-PELCSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:COG0515  10 RILRLLGRGGMGVVYLARDLRLG-----RPVALKVLrPELAADPEARErFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:COG0515  85 VMEYVEGESLADLLRRRGP-------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG---RVKLIDFGIA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDPPR-- 746
Cdd:COG0515 155 RALGGATLTQTGTVVGTPG-YMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSElr 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 747 -GCPGPVYRIMTQCWQHEPELRP-SFASILERLQYCTQDPDVLNSLLPMELGPTPEEEGTSGLGNRSLECLRPPQPQELS 824
Cdd:COG0515 233 pDLPPALDAIVLRALAKDPEERYqSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 312
                       330       340
                ....*....|....*....|...
gi 42544153 825 PEKLKSWGGSPLGPWLSSGLKPL 847
Cdd:COG0515 313 AAAAAAAAAAPAAAAAAAAAAAA 335
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
514-774 1.53e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 67.59  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  514 RALGHGAFGEVyegLVIGLPGDSSPLQVAIKTLpELCSPQD------ELDFLMEALIISkfrhqnIVRCVGLSLRATPR- 586
Cdd:PTZ00283  38 RVLGSGATGTV---LCAKRVSDGEPFAVKVVDM-EGMSEADknraqaEVCCLLNCDFFS------IVKCHEDFAKKDPRn 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  587 -------LILLELMSGGDM----KSFLRHSRPHLGQPSPLVMRDLLqLAqdiaqgCHYLEENHFIHRDIAARNCLLSCAG 655
Cdd:PTZ00283 108 penvlmiALVLDYANAGDLrqeiKSRAKTNRTFREHEAGLLFIQVL-LA------VHHVHSKHMIHRDIKSANILLCSNG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  656 psrVAKIGDFGMARdIYRASYYRRGDRALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGyMPYPGRTNQEVLD 734
Cdd:PTZ00283 181 ---LVKLGDFGFSK-MYAATVSDDVGRTFCGTPyYVAPEIWRRKPYSKKADMFSLGVLLYELLTLK-RPFDGENMEEVMH 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 42544153  735 FVVgGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:PTZ00283 256 KTL-AGRYDPlPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
541-669 4.43e-05

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 47.10  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  541 VAIKTL-PELCSPQDELD-FLMEALIISKFRHQNIVRC--VGlslrATPRL--ILLELMSGGDMKSFLRhsrphlgQPSP 614
Cdd:NF033483  35 VAVKVLrPDLARDPEFVArFRREAQSAASLSHPNIVSVydVG----EDGGIpyIVMEYVDGRTLKDYIR-------EHGP 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153  615 LVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMAR 669
Cdd:NF033483 104 LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIAR 155
 
Name Accession Description Interval E-value
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
503-779 0e+00

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 605.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 503 TEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05036   1 KEVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKI 662
Cdd:cd05036  81 RLPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05036 161 GDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRM 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQY 779
Cdd:cd05036 241 DPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
510-777 2.57e-126

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: 379.92  E-value: 2.57e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   510 VTLLRALGHGAFGEVYEGLVIGlPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKG-EGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   590 LELMSGGDMKSFLRHSRPHLGQPsplvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMAR 669
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLK------DLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE---NLVVKISDFGLSR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   670 DIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCP 749
Cdd:pfam07714 151 DIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCP 230
                         250       260
                  ....*....|....*....|....*...
gi 42544153   750 GPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:pfam07714 231 DELYDLMKQCWAYDPEDRPTFSELVEDL 258
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
516-778 1.41e-123

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: 373.29  E-value: 1.41e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSS-PLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd05044   3 LGSGAFGEVFEGTAKDILGDGSgETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPS-RVAKIGDFGMARDIYR 673
Cdd:cd05044  83 GGDLLSYLRAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYReRVVKIGDFGLARDIYK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVY 753
Cdd:cd05044 163 NDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDDLY 242
                       250       260
                ....*....|....*....|....*
gi 42544153 754 RIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05044 243 ELMLRCWSTDPEERPSFARILEQLQ 267
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
516-778 1.33e-121

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: 368.02  E-value: 1.33e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGdsSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd00192   3 LGEGAFGEVYKGKLKGGDG--KTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHL--GQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMARDIYR 673
Cdd:cd00192  81 GDLLDFLRKSRPVFpsPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLV---GEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVY 753
Cdd:cd00192 158 DDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELY 237
                       250       260
                ....*....|....*....|....*
gi 42544153 754 RIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd00192 238 ELMLSCWQLDPEDRPTFSELVERLE 262
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
510-777 2.45e-119

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 361.85  E-value: 2.45e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    510 VTLLRALGHGAFGEVYEGLVIGLPGDSsPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKK-KVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    590 LELMSGGDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMAR 669
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLS------LSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    670 DIYRASYYR-RGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGC 748
Cdd:smart00219 151 DLYDDDYYRkRGGK--LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNC 228
                          250       260
                   ....*....|....*....|....*....
gi 42544153    749 PGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:smart00219 229 PPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
510-777 5.84e-118

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: 358.40  E-value: 5.84e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    510 VTLLRALGHGAFGEVYEGLVIGLPGDSsPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGK-EVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    590 LELMSGGDMKSFLRHSRPHlgqpsPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMAR 669
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPK-----ELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    670 DIYRASYYR-RGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGC 748
Cdd:smart00221 152 DLYDDDYYKvKGGK--LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNC 229
                          250       260
                   ....*....|....*....|....*....
gi 42544153    749 PGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:smart00221 230 PPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
504-778 2.10e-105

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: 326.61  E-value: 2.10e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05032   2 ELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRP---HLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVA 660
Cdd:cd05032  82 QPTLVVMELMAKGDLKSYLRSRRPeaeNNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVA---EDLTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05032 159 KIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGG 238
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05032 239 HLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
504-778 6.19e-89

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: 283.78  E-value: 6.19e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05061   2 EVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRP----HLGQPSPlVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRV 659
Cdd:cd05061  82 QPTLVVMELMAHGDLKSYLRSLRPeaenNPGRPPP-TLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVA---HDFT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd05061 158 VKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDG 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42544153 740 GRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05061 238 GYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLK 276
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
504-778 1.14e-88

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: 282.73  E-value: 1.14e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFL-RHSrPH---------LGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLsc 653
Cdd:cd05048  81 QPQCMLFEYMAHGDLHEFLvRHS-PHsdvgvssddDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLV-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 654 aGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVL 733
Cdd:cd05048 158 -GDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 734 DFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05048 237 EMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLR 281
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
504-778 3.88e-85

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 273.19  E-value: 3.88e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRPHL-------GQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAgp 656
Cdd:cd05049  81 DPLLMVFEYMEHGDLNKFLRSHGPDAaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 657 sRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFV 736
Cdd:cd05049 159 -LVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECI 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 737 VGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05049 238 TQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
514-778 5.11e-82

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: 263.92  E-value: 5.11e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELM 593
Cdd:cd05041   1 EKIGRGNFGDVYRGVL-----KPDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMARDIYR 673
Cdd:cd05041  76 PGGSLLTFLRKKGARLT------VKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLV---GENNVLKISDFGMSREEED 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVY 753
Cdd:cd05041 147 GEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVY 226
                       250       260
                ....*....|....*....|....*
gi 42544153 754 RIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05041 227 RLMLQCWAYDPENRPSFSEIYNELQ 251
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
504-778 1.51e-80

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 261.12  E-value: 1.51e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05062   2 EVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRPHL-GQP--SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVA 660
Cdd:cd05062  82 QPTLVIMELMTRGDLKSYLRSLRPEMeNNPvqAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVA---EDFTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05062 159 KIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGG 238
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05062 239 LLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIK 276
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
514-777 8.59e-79

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: 255.29  E-value: 8.59e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGLpgdsspLQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGT------TKVAVKTLkPGTMSPEA---FLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMAR--- 669
Cdd:cd05034  72 MSKGSLLDYLRT-----GEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILV---GENNVCKVADFGLARlie 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 -DIYRAsyyRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGC 748
Cdd:cd05034 144 dDEYTA---REGAK--FPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGC 218
                       250       260
                ....*....|....*....|....*....
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05034 219 PDELYDIMLQCWKKEPEERPTFEYLQSFL 247
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
504-778 9.70e-79

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: 255.35  E-value: 9.70e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLpgdssplQVAIKTLPELCSPQDEldFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05039   2 AINKKDLKLGELIGKGEFGDVMLGDYRGQ-------KVAVKCLKDDSTAAQA--FLAEASVMTTLRHPNLVQLLGVVLEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRhSRphlGQpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIG 663
Cdd:cd05039  73 NGLYIVTEYMAKGSLVDYLR-SR---GR-AVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDN---VAKVS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARDiyrASYYRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd05039 145 DFGLAKE---ASSNQDGGK--LPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRME 219
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 744 PPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05039 220 APEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLE 254
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
504-778 1.13e-76

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: 250.90  E-value: 1.13e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05050   1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRPH---------------LGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARN 648
Cdd:cd05050  81 KPMCLLFEYMAYGDLNEFLRHRSPRaqcslshstssarkcGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 649 CLLscaGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRT 728
Cdd:cd05050 161 CLV---GENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMA 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 729 NQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05050 238 HEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
516-778 2.34e-75

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: 246.00  E-value: 2.34e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLvigLPGDSSPlqVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd05084   4 IGRGNFGEVFSGR---LRADNTP--VAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMARDIYRAS 675
Cdd:cd05084  79 GDFLTFLRTEGPRLK------VKELIRMVENAAAGMEYLESKHCIHRDLAARNCLV---TEKNVLKISDFGMSREEEDGV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRI 755
Cdd:cd05084 150 YAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRL 229
                       250       260
                ....*....|....*....|...
gi 42544153 756 MTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05084 230 MEQCWEYDPRKRPSFSTVHQDLQ 252
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
497-777 1.01e-74

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: 246.17  E-value: 1.01e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 497 PLPPgVTEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSS-PLQVAIKTLPELCSPQDELDFL--MEAL-IISKfrHQN 572
Cdd:cd05053   2 PLDP-EWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKPNeVVTVAVKMLKDDATEKDLSDLVseMEMMkMIGK--HKN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 573 IVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSP---------LVMRDLLQLAQDIAQGCHYLEENHFIHRD 643
Cdd:cd05053  79 IINLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPddprvpeeqLTQKDLVSFAYQVARGMEYLASKKCIHRD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 644 IAARNCLLscaGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMP 723
Cdd:cd05053 159 LAARNVLV---TEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSP 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42544153 724 YPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05053 236 YPGIPVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDL 289
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
509-778 1.01e-74

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: 245.65  E-value: 1.01e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPElCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd05092   6 DIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKE-ATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRP--HL-----GQP-SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVA 660
Cdd:cd05092  85 VFEYMRHGDLNRFLRSHGPdaKIldggeGQApGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLV---GQGLVV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05092 162 KIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGR 241
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05092 242 ELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
505-777 4.41e-74

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: 242.74  E-value: 4.41e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLVIGlpgdssPLQVAIKTLPELCSPQDelDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05059   1 IDPSELTFLKELGSGQFGVVHLGKWRG------KIDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRhSRPHLGQpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGD 664
Cdd:cd05059  73 PIFIVTEYMANGCLLNYLR-ERRGKFQ-----TEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLV---GEQNVVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMAR----DIYRASYYRRgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05059 144 FGLARyvldDEYTSSVGTK-----FPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGY 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05059 219 RLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
504-783 1.30e-72

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: 239.23  E-value: 1.30e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLViglpGDSSPlqVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05068   4 EIDRKSLKLLRKLGSGQFGEVWEGLW----NNTTP--VAVKTLkPGTMDPED---FLREAQIMKKLRHPKLIQLYAVCTL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRhsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKI 662
Cdd:cd05068  75 EEPIYIITELMKHGSLLEYLQ------GKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLV---GENNICKV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05068 146 ADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRM 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFasilERLQYCTQD 783
Cdd:cd05068 226 PCPPNCPPQLYDIMLECWKADPMERPTF----ETLQWKLED 262
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
505-778 5.96e-72

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: 237.66  E-value: 5.96e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLvIGLPGdSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05033   1 IDASYVTIEKVIGGGEFGEVCSGS-LKLPG-KKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHsrpHLGQPSPLVmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGD 664
Cdd:cd05033  79 PVMIVTEYMENGSLDKFLRE---NDGKFTVTQ---LVGMLRGIASGMKYLSEMNYVHRDLAARNILVN---SDLVCKVSD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIY--RASYYRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05033 150 FGLSRRLEdsEATYTTKGGK--IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRL 227
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05033 228 PPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLD 263
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
514-780 1.12e-70

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: 233.78  E-value: 1.12e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVigLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLrATPRLILLELM 593
Cdd:cd05060   1 KELGHGNFGSVRKGVY--LMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCK-GEPLMLVMELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLRhSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIyR 673
Cdd:cd05060  78 PLGPLLKYLK-KRREIP------VSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH---QAKISDFGMSRAL-G 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 A--SYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGP 751
Cdd:cd05060 147 AgsDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQE 226
                       250       260
                ....*....|....*....|....*....
gi 42544153 752 VYRIMTQCWQHEPELRPSFASILERLQYC 780
Cdd:cd05060 227 IYSIMLSCWKYRPEDRPTFSELESTFRRD 255
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
516-777 1.76e-69

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: 230.28  E-value: 1.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglpGDSSPlqVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd05085   4 LGKGNFGEVYKGTL----KDKTP--VAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMARD----I 671
Cdd:cd05085  78 GDFLSFLRKKKDELK------TKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLV---GENNALKISDFGMSRQeddgV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYYRRgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGP 751
Cdd:cd05085 149 YSSSGLKQ-----IPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPED 223
                       250       260
                ....*....|....*....|....*.
gi 42544153 752 VYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05085 224 IYKIMQRCWDYNPENRPKFSELQKEL 249
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
510-778 2.86e-68

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: 227.80  E-value: 2.86e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGlpGDSSPLQVAIKTLPELCSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPR-- 586
Cdd:cd05035   1 LKLGKILGEGEFGSVMEAQLKQ--DDGSQLKVAVKTMKVDIHTYSEIeEFLSEAACMKDFDHPNVMRLIGVCFTASDLnk 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 ----LILLELMSGGDMKSFLRHSRPHlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAki 662
Cdd:cd05035  79 ppspMVILPFMKHGDLHSYLLYSRLG-GLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVA-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 gDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05035 156 -DFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRL 234
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05035 235 KQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLE 270
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
510-783 3.97e-68

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: 227.58  E-value: 3.97e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLvigLPGDSSPLQVAIKTLP-ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPR-- 586
Cdd:cd05075   2 LALGKTLGEGEFGSVMEGQ---LNQDDSVLKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESeg 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 ----LILLELMSGGDMKSFLRHSRphLG-QPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAK 661
Cdd:cd05075  79 ypspVVILPFMKHGDLHSFLLYSR--LGdCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLN---ENMNVC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGR 741
Cdd:cd05075 154 VADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNR 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 742 MDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQYCTQD 783
Cdd:cd05075 234 LKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
508-777 1.76e-67

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: 225.81  E-value: 1.76e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 508 ANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL 587
Cdd:cd05046   5 SNLQEITTLGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRP--HLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDF 665
Cdd:cd05046  85 MILEYTDLGDLKQFLRATKSkdEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSS---QREVKVSLL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVL-DFVVGGGRMDP 744
Cdd:cd05046 162 SLSKDVYNSEYYKL-RNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLnRLQAGKLELPV 240
                       250       260       270
                ....*....|....*....|....*....|...
gi 42544153 745 PRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05046 241 PEGCPSRLYKLMTRCWAVNPKDRPSFSELVSAL 273
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
511-777 6.64e-67

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: 223.47  E-value: 6.64e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGLpgdsspLQVAIKTLpelcSPQDEL---DFLMEALIISKFRHQNIVRCVGLSLRATPRL 587
Cdd:cd05148   9 TLERKLGSGYFGEVWEGLWKNR------VRVAIKIL----KSDDLLkqqDFQKEVQALKRLRHKHLISLFAVCSVGEPVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRphlGQPspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGM 667
Cdd:cd05148  79 IITELMEKGSLLAFLRSPE---GQV--LPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILV---GEDLVCKVADFGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 AR----DIYRASYYRrgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd05148 151 ARlikeDVYLSSDKK------IPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMP 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 42544153 744 PPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05148 225 CPAKCPQEIYKIMLECWAAEPEDRPSFKALREEL 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
516-777 2.54e-66

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: 221.26  E-value: 2.54e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPgdssplqVAIKTL-PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTD-------VAIKKLkVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRhsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIyrA 674
Cdd:cd13999  74 GGSLYDLLH------KKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENF---TVKIADFGLSRIK--N 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 675 SYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRM-DPPRGCPGPVY 753
Cdd:cd13999 143 STTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAAAVVQKGLRpPIPPDCPPELS 221
                       250       260
                ....*....|....*....|....
gi 42544153 754 RIMTQCWQHEPELRPSFASILERL 777
Cdd:cd13999 222 KLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
511-778 5.72e-66

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: 222.10  E-value: 5.72e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVigLPGDSSPLQVAIKTL-PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPR--- 586
Cdd:cd05074  12 TLGRMLGKGEFGSVREAQL--KSEDGSFQKVAVKMLkADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKgrl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 ---LILLELMSGGDMKSFLRHSRphLGQ-PSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKI 662
Cdd:cd05074  90 pipMVILPFMKHGDLHTFLLMSR--IGEePFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLN---ENMTVCV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05074 165 ADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLIKGNRL 244
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05074 245 KQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLE 280
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
509-778 1.01e-65

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: 221.45  E-value: 1.01e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPElCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd05093   6 NIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPHL------GQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKI 662
Cdd:cd05093  85 VFEYMKHGDLNKFLRAHGPDAvlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05093 162 GDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05093 242 QRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQ 277
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
509-778 1.28e-65

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: 219.74  E-value: 1.28e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPgdssplqVAIKTLPELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLRaTPRLI 588
Cdd:cd05083   7 KLTLGEIIGEGEFGAVLQGEYMGQK-------VAVKNIKCDVTAQA---FLEETAVMTKLQHKNLVRLLGVILH-NGLYI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRhSRPHLGQPSPlvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:cd05083  76 VMELMSKGNLVNFLR-SRGRALVPVI----QLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG---VAKISDFGLA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASyyrrgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGC 748
Cdd:cd05083 148 KVGSMGV-----DNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGC 222
                       250       260       270
                ....*....|....*....|....*....|
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05083 223 PPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
509-778 1.75e-65

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 221.06  E-value: 1.75e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVY----EGLVIGLPGDS-------SPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCV 577
Cdd:cd05051   6 KLEFVEKLGEGQFGEVHlceaNGLSDLTSDDFigndnkdEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 578 GLSLRATPRLILLELMSGGDMKSFLRH-----SRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLs 652
Cdd:cd05051  86 GVCTRDEPLCMIVEYMENGDLNQFLQKheaetQGASATNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLV- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 653 caGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGY-MPYPGRTNQE 731
Cdd:cd05051 165 --GPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKeQPYEHLTDEQ 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42544153 732 VLD-----FVVGGGR--MDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05051 243 VIEnagefFRDDGMEvyLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQ 296
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
504-778 6.92e-65

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: 218.06  E-value: 6.92e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPELCSPQDEldFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05052   2 EIERTDITMKHKLGGGQYGEVYEGV-----WKKYNLTVAVKTLKEDTMEVEE--FLKEAAVMKEIKHPNLVQLLGVCTRE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRhsRPHLGQPSPLVmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIG 663
Cdd:cd05052  75 PPFYIITEFMPYGNLLDYLR--ECNREELNAVV---LLYMATQIASAMEYLEKKNFIHRDLAARNCLV---GENHLVKVA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMAR----DIYRAsyyRRGdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd05052 147 DFGLSRlmtgDTYTA---HAG--AKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKG 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42544153 740 GRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05052 222 YRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
505-777 1.32e-64

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: 217.13  E-value: 1.32e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLVIglpgdsSPLQVAIKTLPElcSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05112   1 IDPSELTFVQEIGSGQFGLVHLGYWL------NKDKVAIKTIRE--GAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHLGQPSplvmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGD 664
Cdd:cd05112  73 PICLVFEFMEHGCLSDYLRTQRGLFSAET------LLGMCLDVCEGMAYLEEASVIHRDLAARNCLV---GENQVVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMAR----DIYRASYYRRgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05112 144 FGMTRfvldDQYTSSTGTK-----FPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGF 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05112 219 RLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
510-778 2.41e-64

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: 217.49  E-value: 2.41e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVigLPGDSSPLQVAIKTLPELCSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRATPR-- 586
Cdd:cd14204   9 LSLGKVLGEGEFGSVMEGEL--QQPDGTNHKVAVKTMKLDNFSQREIEeFLSEAACMKDFNHPNVIRLLGVCLEVGSQri 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 ---LILLELMSGGDMKSFLRHSRPHLGqPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIG 663
Cdd:cd14204  87 pkpMVILPFMKYGDLHSFLLRSRLGSG-PQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLR---DDMTVCVA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd14204 163 DFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGHRLK 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 744 PPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14204 243 QPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLE 277
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
509-778 5.43e-64

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: 216.75  E-value: 5.43e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSR---------------PHLGQPS--PLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL 651
Cdd:cd05045  81 IVEYAKYGSLRSFLRESRkvgpsylgsdgnrnsSYLDNPDerALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 ScagPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQE 731
Cdd:cd05045 161 A---EGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPER 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 732 VLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05045 238 LFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELE 284
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
509-778 7.76e-64

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 216.97  E-value: 7.76e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPElCSPQDELDFLMEAL-IISKF-RHQNIVRCVGLSLRATPR 586
Cdd:cd05055  36 NLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKP-TAHSSEREALMSELkIMSHLgNHENIVNLLGACTIGGPI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHSRPHLgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLsCAGpsRVAKIGDFG 666
Cdd:cd05055 115 LVITEYCCYGDLLNFLRRKRESF-----LTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL-THG--KIVKICDFG 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGR-TNQEVLDFVVGGGRMDPP 745
Cdd:cd05055 187 LARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMpVDSKFYKLIKEGYRMAQP 266
                       250       260       270
                ....*....|....*....|....*....|...
gi 42544153 746 RGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05055 267 EHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIG 299
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
504-778 8.98e-64

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: 216.03  E-value: 8.98e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIgLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIYKGHLY-LPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRPH--LG--------QPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLsc 653
Cdd:cd05090  80 QPVCMLFEFMNQGDLHEFLIMRSPHsdVGcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILV-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 654 aGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVL 733
Cdd:cd05090 158 -GEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 734 DFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05090 237 EMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLR 281
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
509-777 7.38e-63

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: 214.44  E-value: 7.38e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGD--SSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRATP 585
Cdd:cd05099  13 RLVLGKPLGEGCFGQVVRAEAYGIDKSrpDQTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMSGGDMKSFLRHSRPhlgqPSP-------------LVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS 652
Cdd:cd05099  93 LYVIVEYAAKGNLREFLRARRP----PGPdytfditkvpeeqLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 653 cagPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEV 732
Cdd:cd05099 169 ---EDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEEL 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 733 LDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05099 246 FKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEAL 290
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
504-777 2.08e-62

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: 211.90  E-value: 2.08e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSspLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLsLRA 583
Cdd:cd05056   2 EIQREDITLGRCIGEGQFGDVYQGVYMSPENEK--IAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGV-ITE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHSRphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscAGPSRVaKIG 663
Cdd:cd05056  79 NPVWIVMELAPLGELRSYLQVNK------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSPDCV-KLG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARDIYRASYYRrGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd05056 150 DFGLSRYMEDESYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLP 228
                       250       260       270
                ....*....|....*....|....*....|....
gi 42544153 744 PPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05056 229 MPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
514-778 7.01e-62

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: 210.02  E-value: 7.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIglPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLR--ATPrLILLE 591
Cdd:cd05058   1 EVIGKGHFGCVYHGTLI--DSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPseGSP-LVVLP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSrphlgQPSPLVmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDI 671
Cdd:cd05058  78 YMKHGDLRNFIRSE-----THNPTV-KDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLD---ESFTVKVADFGLARDI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYY--RRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCP 749
Cdd:cd05058 149 YDKEYYsvHNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCP 228
                       250       260
                ....*....|....*....|....*....
gi 42544153 750 GPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05058 229 DPLYEVMLSCWHPKPEMRPTFSELVSRIS 257
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
504-812 8.90e-62

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: 212.19  E-value: 8.90e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGD--SSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLS 580
Cdd:cd05100   8 ELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDkpNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 581 LRATPRLILLELMSGGDMKSFLRHSRPHLGQPS---------PLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL 651
Cdd:cd05100  88 TQDGPLYVLVEYASKGNLREYLRARRPPGMDYSfdtcklpeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 ScagPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQE 731
Cdd:cd05100 168 T---EDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 732 VLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILE---RLQYCTQDPDVLNSLLPME-LGPT-PEEEGTSG 806
Cdd:cd05100 245 LFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEdldRVLTVTSTDEYLDLSVPFEqYSPGcPDSPSSCS 324

                ....*.
gi 42544153 807 LGNRSL 812
Cdd:cd05100 325 SGDDSV 330
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
516-784 9.26e-62

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: 210.35  E-value: 9.26e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIgLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILlELMSG 595
Cdd:cd05057  15 LGSGAFGTVYKGVWI-PEGEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQLIT-QLMPL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagPSRVaKIGDFGMARDIYRAS 675
Cdd:cd05057  93 GCLLDYVRNHRDNIGS------QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKT--PNHV-KITDFGLAKLLDVDE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRI 755
Cdd:cd05057 164 KEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTIDVYMV 243
                       250       260
                ....*....|....*....|....*....
gi 42544153 756 MTQCWQHEPELRPSFASILERLQYCTQDP 784
Cdd:cd05057 244 LVKCWMIDAESRPTFKELANEFSKMARDP 272
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
504-777 1.57e-61

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: 209.44  E-value: 1.57e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGlVIGLPGDSSpLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05063   1 EIHPSHITKQKVIGAGEFGEVFRG-ILKMPGRKE-VAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHsrpHLGQPSPLvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIG 663
Cdd:cd05063  79 KPAMIITEYMENGALDKYLRD---HDGEFSSY---QLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVN---SNLECKVS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMAR---DIYRASYYRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05063 150 DFGLSRvleDDPEGTYTTSGGK--IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGF 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFA---SILERL 777
Cdd:cd05063 228 RLPAPMDCPSAVYQLMLQCWQQDRARRPRFVdivNLLDKL 267
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
505-779 7.05e-61

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: 207.02  E-value: 7.05e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGevyeglVIGLPGDSSPLQVAIKTLPElcSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05114   1 INPSELTFMKELGSGLFG------VVRLGKWRAQYKVAIKAIRE--GAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHLGqpsplvmRD-LLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIG 663
Cdd:cd05114  73 PIYIVTEFMENGCLLNYLRQRRGKLS-------RDmLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTG---VVKVS 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARDIYRASYYRRGDrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd05114 143 DFGMTRYVLDDQYTSSSG-AKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLY 221
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 744 PPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQY 779
Cdd:cd05114 222 RPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTITE 257
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
509-777 1.41e-60

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 207.17  E-value: 1.41e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTL--PELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLRATPR 586
Cdd:cd05094   6 DIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLkdPTLAARKD---FQREAELLTNLQHDHIVKFYGVCGDGDPL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHSRPHL-----GQP----SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPS 657
Cdd:cd05094  83 IMVFEYMKHGDLNKFLRAHGPDAmilvdGQPrqakGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLV---GAN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 RVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVV 737
Cdd:cd05094 160 LLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECIT 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 738 GGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05094 240 QGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKIL 279
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
490-777 3.00e-60

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: 207.56  E-value: 3.00e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 490 LGPAQSWPLPPGVT-EVSPANVTLLRALGHGAFGEVYEGLVIGLPGD--SSPLQVAIKTLPELCSPQDELDFLMEALIIS 566
Cdd:cd05101   5 LAGVSEYELPEDPKwEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDkpKEAVTVAVKMLKDDATEKDLSDLVSEMEMMK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 567 KF-RHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPS---------PLVMRDLLQLAQDIAQGCHYLEE 636
Cdd:cd05101  85 MIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSydinrvpeeQMTFKDLVSCTYQLARGMEYLAS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 637 NHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEI 716
Cdd:cd05101 165 QKCIHRDLAARNVLVT---ENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEI 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 717 FSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05101 242 FTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 302
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
504-777 5.91e-60

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: 206.02  E-value: 5.91e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGD--SSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLS 580
Cdd:cd05098   9 ELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDkpNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGAC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 581 LRATPRLILLELMSGGDMKSFLRHSRP----HLGQPS-----PLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL 651
Cdd:cd05098  89 TQDGPLYVIVEYASKGNLREYLQARRPpgmeYCYNPShnpeeQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 ScagPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQE 731
Cdd:cd05098 169 T---EDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEE 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 732 VLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05098 246 LFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 291
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
509-779 8.14e-60

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: 204.06  E-value: 8.14e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVyeglvigLPGDSSPLQVAIKTLPELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLRATPRL- 587
Cdd:cd05082   7 ELKLLQTIGKGEFGDV-------MLGDYRGNKVAVKCIKNDATAQA---FLAEASVMTQLRHSNLVQLLGVIVEEKGGLy 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLR-HSRPHLGQPSplvmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFG 666
Cdd:cd05082  77 IVTEYMAKGSLVDYLRsRGRSVLGGDC------LLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVS---EDNVAKVSDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASyyrrgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPR 746
Cdd:cd05082 148 LTKEASSTQ-----DTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPD 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 42544153 747 GCPGPVYRIMTQCWQHEPELRPSFASILERLQY 779
Cdd:cd05082 223 GCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEH 255
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
507-773 9.60e-58

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: 199.82  E-value: 9.60e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANVTLLR-ALGHGAFGEVY----EGLV--IGLPG---DSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRC 576
Cdd:cd05097   3 PRQQLRLKeKLGEGQFGEVHlceaEGLAefLGEGApefDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 577 VGLSLRATPRLILLELMSGGDMKSFL--RHSRPHLGQPS--PLVMR-DLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL 651
Cdd:cd05097  83 LGVCVSDDPLCMITEYMENGDLNQFLsqREIESTFTHANniPSVSIaNLLYMAVQIASGMKYLASLNFVHRDLATRNCLV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 scaGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL-GYMPYPGRTNQ 730
Cdd:cd05097 163 ---GNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSLLSDE 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 731 EVL----DFVVGGGR---MDPPRGCPGPVYRIMTQCWQHEPELRPSFASI 773
Cdd:cd05097 240 QVIentgEFFRNQGRqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
514-777 1.05e-57

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 199.64  E-value: 1.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVG-LSLRATPRLILLE 591
Cdd:cd05054  13 KPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGaCTKPGGPLMVIVE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSR----------PHLGQP---------SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS 652
Cdd:cd05054  93 FCKFGNLSNYLRSKReefvpyrdkgARDVEEeedddelykEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLS 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 653 cagPSRVAKIGDFGMARDIYR-ASYYRRGDrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPG-RTNQ 730
Cdd:cd05054 173 ---ENNVVKICDFGLARDIYKdPDYVRKGD-ARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGvQMDE 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 731 EVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05054 249 EFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
505-778 1.78e-57

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: 197.80  E-value: 1.78e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLVIGlpgdssPLQVAIKTLPELCSPQDEldFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYGKWRG------QYDVAIKMIKEGSMSEDE--FIEEAKVMMNLSHEKLVQLYGVCTKQR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHLgQPSplvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGD 664
Cdd:cd05113  73 PIFIITEYMANGCLLNYLREMRKRF-QTQ-----QLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQG---VVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMAR----DIYRASYYRRgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05113 144 FGLSRyvldDEYTSSVGSK-----FPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGL 218
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05113 219 RLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNIL 256
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
509-778 3.32e-57

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 200.84  E-value: 3.32e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPqDELDFLMEAL-IISKF-RHQNIVRCVGLSLRATPR 586
Cdd:cd05106  39 NLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASAHT-DEREALMSELkILSHLgQHKNIVNLLGACTHGGPV 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHS------------------------------------------------RPHLGQPS----- 613
Cdd:cd05106 118 LVITEYCCYGDLLNFLRKKaetflnfvmalpeisetssdyknitlekkyirsdsgfssqgsdtyvemRPVSSSSSqssds 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 614 ----------PLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYRASYYRRGDRA 683
Cdd:cd05106 198 kdeedtedswPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLT---DGRVAKICDFGLARDIMNDSNYVVKGNA 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 684 LLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPG-RTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQH 762
Cdd:cd05106 275 RLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGiLVNSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNL 354
                       330
                ....*....|....*.
gi 42544153 763 EPELRPSFASILERLQ 778
Cdd:cd05106 355 EPTERPTFSQISQLIQ 370
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
504-778 3.97e-57

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 197.55  E-value: 3.97e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIG-LPGDSSPLqVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05091   2 EINLSAVRFMEELGEDRFGKVYKGHLFGtAPGEQTQA-VAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRHSRPH--LGQP-------SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSc 653
Cdd:cd05091  81 EQPMSMIFSYCSHGDLHEFLVMRSPHsdVGSTdddktvkSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVF- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 654 agPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVL 733
Cdd:cd05091 160 --DKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVI 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 734 DFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05091 238 EMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRLR 282
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
504-782 6.95e-57

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: 196.80  E-value: 6.95e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLViglpgdSSPLQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05072   3 EIPRESIKLVKKLGAGQFGEVWMGYY------NNSTKVAVKTLkPGTMSVQA---FLEEANLMKTLQHDKLVRLYAVVTK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRHSrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKI 662
Cdd:cd05072  74 EEPIYIITEYMAKGSLLDFLKSD-----EGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVS---ESLMCKI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05072 146 ADFGLARVIEDNEYTAR-EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRM 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSF---ASILERLQYCTQ 782
Cdd:cd05072 225 PRMENCPDELYDIMKTCWKEKAEERPTFdylQSVLDDFYTATE 267
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
504-775 2.26e-56

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: 194.72  E-value: 2.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGlpgdssPLQVAIKTLPE-LCSPQDeldFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05067   3 EVPRETLKLVERLGAGQFGEVWMGYYNG------HTKVAIKSLKQgSMSPDA---FLAEANLMKQLQHQRLVRLYAVVTQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 AtPRLILLELMSGGDMKSFLRHSRPHlgqpsPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKI 662
Cdd:cd05067  74 E-PIYIITEYMENGSLVDFLKTPSGI-----KLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVS---DTLSCKI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05067 145 ADFGLARLIEDNEYTAR-EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRM 223
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFA---SILE 775
Cdd:cd05067 224 PRPDNCPEELYQLMRLCWKERPEDRPTFEylrSVLE 259
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
516-777 1.13e-55

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: 192.56  E-value: 1.13e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSspLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLrATPRLILLELM 593
Cdd:cd05040   3 LGDGSFGVVRRGEWTTPSGKV--IQVAVKCLKSdvLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVL-SSPLMMVTELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLRHSRPHLgqpspLVMRdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscAGPSRVaKIGDFGMAR---- 669
Cdd:cd05040  80 PLGSLLDRLRKDQGHF-----LIST-LCDYAVQIANGMAYLESKRFIHRDLAARNILL--ASKDKV-KIGDFGLMRalpq 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 --DIYRASYYRRgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFV-VGGGRMDPPR 746
Cdd:cd05040 151 neDHYVMQEHRK-----VPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIdKEGERLERPD 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 42544153 747 GCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05040 226 DCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
505-777 1.57e-55

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: 192.77  E-value: 1.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLvIGLPGDSSpLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05066   1 IDASCIKIEKVIGAGEFGEVCSGR-LKLPGKRE-IPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHsrpHLGQpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGD 664
Cdd:cd05066  79 PVMIVTEYMENGSLDAFLRK---HDGQ---FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVN---SNLVCKVSD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMAR---DIYRASYYRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGR 741
Cdd:cd05066 150 FGLSRvleDDPEAAYTTRGGK--IPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYR 227
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 742 MDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05066 228 LPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSIL 263
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
504-773 2.90e-55

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


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 192.06  E-value: 2.90e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGlVIGLPGDSSpLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05064   1 ELDNKSIKIERILGTGRFGELCRG-CLKLPSKRE-LPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHsrpHLGQpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIG 663
Cdd:cd05064  79 NTMMIVTEYMSNGALDSFLRK---HEGQ---LVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVN---SDLVCKIS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFG-MARDIYRASYYRRGDRAllPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05064 150 GFRrLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRL 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASI 773
Cdd:cd05064 228 PAPRNCPNLLHQLMLDCWQKERGERPRFSQI 258
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
504-777 8.22e-55

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 192.89  E-value: 8.22e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLME-ALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05102   3 EFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSElKILIHIGNHLNVVNLLGACTK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 AT-PRLILLELMSGGDMKSFLRHSR----------PHL----------------------------------GQP----- 612
Cdd:cd05102  83 PNgPLMVIVEFCKYGNLSNFLRAKRegfspyrersPRTrsqvrsmveavradrrsrqgsdrvasftestsstNQPrqevd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 613 ----SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYRASYYRRGDRALLPVK 688
Cdd:cd05102 163 dlwqSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLS---ENNVVKICDFGLARDIYKDPDYVRKGSARLPLK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 689 WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPG-RTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELR 767
Cdd:cd05102 240 WMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGvQINEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKER 319
                       330
                ....*....|
gi 42544153 768 PSFASILERL 777
Cdd:cd05102 320 PTFSDLVEIL 329
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
514-783 9.91e-55

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: 189.74  E-value: 9.91e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGlpgdssPLQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLsLRATPRLILLEL 592
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNG------TTKVAIKTLkPGTMSPEA---FLEEAQIMKKLRHDKLVQLYAV-VSEEPIYIVTEF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMARDIY 672
Cdd:cd14203  71 MSKGSLLDFLKD-----GEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILV---GDNLVCKIADFGLARLIE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPV 752
Cdd:cd14203 143 DNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESL 221
                       250       260       270
                ....*....|....*....|....*....|.
gi 42544153 753 YRIMTQCWQHEPELRPSFasilERLQYCTQD 783
Cdd:cd14203 222 HELMCQCWRKDPEERPTF----EYLQSFLED 248
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
516-777 1.74e-54

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: 189.87  E-value: 1.74e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd05047   3 IGEGNFGQVLKARI---KKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSR-----PHL----GQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDF 665
Cdd:cd05047  80 HGNLLDFLRKSRvletdPAFaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDiyrASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPP 745
Cdd:cd05047 157 GLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKP 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 746 RGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05047 234 LNCDDEVYDLMRQCWREKPYERPSFAQILVSL 265
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
510-778 2.30e-54

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: 190.59  E-value: 2.30e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVY----EGLVIGLPGD-------SSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVG 578
Cdd:cd05095   7 LTFKEKLGEGQFGEVHlceaEGMEKFMDKDfalevseNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 579 LSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMR-----DLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLsc 653
Cdd:cd05095  87 VCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALPSNALtvsysDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLV-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 654 aGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL-GYMPYPGRTNQEV 732
Cdd:cd05095 165 -GKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPYSQLSDEQV 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42544153 733 L----DFVVGGGR---MDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05095 244 IentgEFFRDQGRqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQ 296
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
509-777 3.21e-54

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: 189.51  E-value: 3.21e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGlVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLS---LRATP 585
Cdd:cd05038   5 HLKFIKQLGEGHFGSVELC-RYDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCespGRRSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILlELMSGGDMKSFLRHSRPHLGQPSplvmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDF 665
Cdd:cd05038  84 RLIM-EYLPSGSLRDYLQRHRDQIDLKR------LLLFASQICKGMEYLGSQRYIHRDLAARNILVE---SEDLVKISDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRAS-YYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLG-----------YMPYPGRTNQEVL 733
Cdd:cd05038 154 GLAKVLPEDKeYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqsppalflRMIGIAQGQMIVT 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 734 DFV---VGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05038 234 RLLellKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILII 280
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
509-778 6.83e-54

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: 189.05  E-value: 6.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLViglPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRATPRL 587
Cdd:cd05089   3 DIKFEDVIGEGNFGQVIKAMI---KKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSR---------PHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSR 658
Cdd:cd05089  80 IAIEYAPYGNLLDFLRKSRvletdpafaKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLV---GENL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 659 VAKIGDFGMARDiyrASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVG 738
Cdd:cd05089 157 VSKIADFGLSRG---EEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42544153 739 GGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASI---LERLQ 778
Cdd:cd05089 234 GYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQIsvqLSRML 276
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
504-777 6.45e-53

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 187.90  E-value: 6.45e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQ-NIVRCVGLSLR 582
Cdd:cd14207   3 EFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLLGACTK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 -ATPRLILLELMSGGDMKSFLRHSR-----------------------PHLGQ-------PS------------------ 613
Cdd:cd14207  83 sGGPLMVIVEYCKYGNLSNYLKSKRdffvtnkdtslqeelikekkeaePTGGKkkrlesvTSsesfassgfqedkslsdv 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 614 -------------PLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYR-ASYYRR 679
Cdd:cd14207 163 eeeeedsgdfykrPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLS---ENNVVKICDFGLARDIYKnPDYVRK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 680 GDrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPG-RTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQ 758
Cdd:cd14207 240 GD-ARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGvQIDEDFCSKLKEGIRMRAPEFATSEIYQIMLD 318
                       330
                ....*....|....*....
gi 42544153 759 CWQHEPELRPSFASILERL 777
Cdd:cd14207 319 CWQGDPNERPRFSELVERL 337
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
513-784 8.09e-53

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 185.61  E-value: 8.09e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGlvIGLP-GDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILlE 591
Cdd:cd05109  12 VKVLGSGAFGTVYKG--IWIPdGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQLVT-Q 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFGMAR-- 669
Cdd:cd05109  89 LMPYGCLLDYVRENKDRIGS------QDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVK--SPNHV-KITDFGLARll 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRASYYRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCP 749
Cdd:cd05109 160 DIDETEYHADGGK--VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICT 237
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 750 GPVYRIMTQCWQHEPELRPSFASILERLQYCTQDP 784
Cdd:cd05109 238 IDVYMIMVKCWMIDSECRPRFRELVDEFSRMARDP 272
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
516-773 8.51e-53

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: 186.29  E-value: 8.51e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVY--------EGLVIGLPGD---SSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05096  13 LGEGQFGEVHlcevvnpqDLPTLQFPFNvrkGRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVDED 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRH---------SRPHLGQPSPLVM---RDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLs 652
Cdd:cd05096  93 PLCMITEYMENGDLNQFLSShhlddkeenGNDAVPPAHCLPAisySSLLHVALQIASGMKYLSSLNFVHRDLATRNCLV- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 653 caGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL-GYMPYPGRTNQE 731
Cdd:cd05096 172 --GENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKEQPYGELTDEQ 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42544153 732 VLD----FVVGGGR---MDPPRGCPGPVYRIMTQCWQHEPELRPSFASI 773
Cdd:cd05096 250 VIEnageFFRDQGRqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
505-777 2.17e-52

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: 183.92  E-value: 2.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLvIGLPGDSSpLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05065   1 IDVSCVKIEEVIGAGEFGEVCRGR-LKLPGKRE-IFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRphlGQPSPLvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGD 664
Cdd:cd05065  79 PVMIITEFMENGALDSFLRQND---GQFTVI---QLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVN---SNLVCKVSD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRAS---YYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGR 741
Cdd:cd05065 150 FGLSRFLEDDTsdpTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYR 229
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 742 MDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05065 230 LPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTL 265
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
513-802 2.07e-51

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: 182.91  E-value: 2.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIGlPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILlEL 592
Cdd:cd05108  12 IKVLGSGAFGTVYKGLWIP-EGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIT-QL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFGMARDIY 672
Cdd:cd05108  90 MPFGCLLDYVREHKDNIGS------QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK--TPQHV-KITDFGLAKLLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPV 752
Cdd:cd05108 161 AEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDV 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42544153 753 YRIMTQCWQHEPELRPSFASILERLQYCTQDPD---VLNSLLPMELgPTPEEE 802
Cdd:cd05108 241 YMIMVKCWMIDADSRPKFRELIIEFSKMARDPQrylVIQGDERMHL-PSPTDS 292
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
512-777 2.37e-51

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 183.64  E-value: 2.37e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQ-NIVRCVG-LSLRATPRLIL 589
Cdd:cd05103  11 LGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLLGaCTKPGGPLMVI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSR----PHLGQ------------------------------------------------------ 611
Cdd:cd05103  91 VEFCKFGNLSAYLRSKRsefvPYKTKgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsdveeeeagqed 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 612 --PSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYR-ASYYRRGDrALLPVK 688
Cdd:cd05103 171 lyKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLS---ENNVVKICDFGLARDIYKdPDYVRKGD-ARLPLK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 689 WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPG-RTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELR 767
Cdd:cd05103 247 WMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGvKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQR 326
                       330
                ....*....|
gi 42544153 768 PSFASILERL 777
Cdd:cd05103 327 PTFSELVEHL 336
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
505-783 1.45e-50

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: 179.18  E-value: 1.45e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 505 VSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSplQVAIKTLPELCSPQDELDFLMEALIISKFRHQNI--VRCVGLSLR 582
Cdd:cd05043   3 VSRERVTLSDLLQEGTFGRIFHGILRDEKGKEE--EVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLlpILHVCIEDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPrLILLELMSGGDMKSFLRHSR-PHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscAGPSRVaK 661
Cdd:cd05043  81 EKP-MVLYPYMNWGNLKLFLQQCRlSEANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVI--DDELQV-K 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGR 741
Cdd:cd05043 157 ITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYR 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 742 MDPPRGCPGPVYRIMTQCWQHEPELRPSFasilERLQYCTQD 783
Cdd:cd05043 237 LAQPINCPDELFAVMACCWALDPEERPSF----QQLVQCLTD 274
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
504-778 5.49e-49

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 174.87  E-value: 5.49e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPgdssplQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLsLR 582
Cdd:cd05069   8 EIPRESLRLDVKLGQGCFGEVWMGTWNGTT------KVAIKTLkPGTMMPEA---FLQEAQIMKKLRHDKLVPLYAV-VS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRHsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKI 662
Cdd:cd05069  78 EEPIYIVTEFMGKGSLLDFLKE-----GDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILV---GDNLVCKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05069 150 ADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRM 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05069 229 PCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
502-783 4.18e-48

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: 172.18  E-value: 4.18e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 502 VTEVSPANVTLLRALGHGAFGEVYEGLVIGlpgdssPLQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLS 580
Cdd:cd05070   3 VWEIPRESLQLIKRLGNGQFGEVWMGTWNG------NTKVAIKTLkPGTMSPES---FLEEAQIMKKLKHDKLVQLYAVV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 581 LRaTPRLILLELMSGGDMKSFLRHsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVA 660
Cdd:cd05070  74 SE-EPIYIVTEYMSKGSLLDFLKD-----GEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILV---GNGLIC 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd05070 145 KIADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGY 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELRPSFasilERLQYCTQD 783
Cdd:cd05070 224 RMPCPQDCPISLHELMIHCWKKDPEERPTF----EYLQGFLED 262
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
504-775 6.07e-48

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: 171.36  E-value: 6.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYeglvigLPGDSSPLQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd05073   7 EIPRESLKLEKKLGAGQFGEVW------MATYNKHTKVAVKTMkPGSMSVEA---FLAEANVMKTLQHDKLVKLHAVVTK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 AtPRLILLELMSGGDMKSFLRHSRphlGQPSPLvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAgpsRVAKI 662
Cdd:cd05073  78 E-PIYIITEFMAKGSLLDFLKSDE---GSKQPL--PKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSAS---LVCKI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd05073 149 ADFGLARVIEDNEYTAR-EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRM 227
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 743 DPPRGCPGPVYRIMTQCWQHEPELRPSF---ASILE 775
Cdd:cd05073 228 PRPENCPEELYNIMMRCWKNRPEERPTFeyiQSVLD 263
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
516-778 6.14e-48

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: 170.91  E-value: 6.14e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSSplqVAIKTL------PELcspQDELdfLMEALIISKFRHQNIVRCVGLSlRATPRLIL 589
Cdd:cd05116   3 LGSGNFGTVKKGYYQMKKVVKT---VAVKILkneandPAL---KDEL--LREANVMQQLDNPYIVRMIGIC-EAESWMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRpHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMAR 669
Cdd:cd05116  74 MEMAELGPLNKFLQKNR-HVTE------KNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVT---QHYAKISDFGLSK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYR-ASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGC 748
Cdd:cd05116 144 ALRAdENYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGC 223
                       250       260       270
                ....*....|....*....|....*....|
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05116 224 PPEMYDLMKLCWTYDVDERPGFAAVELRLR 253
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
516-780 7.86e-48

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: 171.28  E-value: 7.86e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLvigLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSlRATPRLILLELMSG 595
Cdd:cd05115  12 LGSGNFGCVKKGV---YKMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVMEMASG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLrhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDI-YRA 674
Cdd:cd05115  88 GPLNKFL------SGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLV---NQHYAKISDFGLSKALgADD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 675 SYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYR 754
Cdd:cd05115 159 SYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYA 238
                       250       260
                ....*....|....*....|....*.
gi 42544153 755 IMTQCWQHEPELRPSFASILERLQYC 780
Cdd:cd05115 239 LMSDCWIYKWEDRPNFLTVEQRMRTY 264
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
504-770 1.02e-47

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 171.02  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPgdssplQVAIKTL-PELCSPQDeldFLMEALIISKFRHQNIVRCVGLsLR 582
Cdd:cd05071   5 EIPRESLRLEVKLGQGCFGEVWMGTWNGTT------RVAIKTLkPGTMSPEA---FLQEAQVMKKLRHEKLVQLYAV-VS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRhsrphlGQPSPLV-MRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAK 661
Cdd:cd05071  75 EEPIYIVTEYMSKGSLLDFLK------GEMGKYLrLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILV---GENLVCK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRASYYRRgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGR 741
Cdd:cd05071 146 VADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYR 224
                       250       260
                ....*....|....*....|....*....
gi 42544153 742 MDPPRGCPGPVYRIMTQCWQHEPELRPSF 770
Cdd:cd05071 225 MPCPPECPESLHDLMCQCWRKEPEERPTF 253
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
514-778 1.22e-47

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 173.94  E-value: 1.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTL-PELCSPQDELdfLMEALIISKF--RHQNIVRCVGLSLRATPRLILL 590
Cdd:cd05104  41 KTLGAGAFGKVVEATAYGLAKADSAMTVAVKMLkPSAHSTEREA--LMSELKVLSYlgNHINIVNLLGACTVGGPTLVIT 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHL---------------------------------GQPSP----------------------- 614
Cdd:cd05104 119 EYCCYGDLLNFLRRKRDSFicpkfedlaeaalyrnllhqremacdslneymdMKPSVsyvvptkadkrrgvrsgsyvdqd 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 615 ------------LVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYRASYYRRGDR 682
Cdd:cd05104 199 vtseileedelaLDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLT---HGRITKICDFGLARDIRNDSNYVVKGN 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 683 ALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGR-TNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQ 761
Cdd:cd05104 276 ARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMpVDSKFYKMIKEGYRMDSPEFAPSEMYDIMRSCWD 355
                       330
                ....*....|....*..
gi 42544153 762 HEPELRPSFASILERLQ 778
Cdd:cd05104 356 ADPLKRPTFKQIVQLIE 372
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
510-793 2.11e-47

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 174.06  E-value: 2.11e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRATPRLI 588
Cdd:cd05105  39 LVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLgPHLNIVNLLGACTKSGPIYI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPHLGQPSP------------------------------------------------------ 614
Cdd:cd05105 119 ITEYCFYGDLVNYLHKNRDNFLSRHPekpkkdldifginpadestrsyvilsfenkgdymdmkqadttqyvpmleikeas 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 615 -----------------------------------LVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRV 659
Cdd:cd05105 199 kysdiqrsnydrpasykgsndsevknllsddgsegLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLA---QGKI 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGR-TNQEVLDFVVG 738
Cdd:cd05105 276 VKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMiVDSTFYNKIKS 355
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 739 GGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASIlerlqyctqdPDVLNSLLPM 793
Cdd:cd05105 356 GYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHL----------SDIVESLLPS 400
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
513-779 8.30e-47

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: 168.59  E-value: 8.30e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd14206   2 LQEIGNGWFGKVILGEIFS---DYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHSRPHLGQPSPLVMRDLLQL---AQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMAR 669
Cdd:cd14206  79 CQLGDLKRYLRAQRKADGMTPDLPTRDLRTLqrmAYEITLGLLHLHKNNYIHSDLALRNCLLT---SDLTVRIGDYGLSH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRASYYRRGDRALLPVKWMPPEAF--LEGIF-----TSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd14206 156 NNYKEDYYLTPDRLWIPLRWVAPELLdeLHGNLivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVVREQQM 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 743 ---DPPRGCPGP--VYRIMTQCWQhEPELRPSFASILERLQY 779
Cdd:cd14206 236 klaKPRLKLPYAdyWYEIMQSCWL-PPSQRPSVEELHLQLSY 276
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
516-779 2.08e-46

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: 166.99  E-value: 2.08e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd05042   3 IGNGWFGKVLLGEIYS---GTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQPSPLvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMARDIYRAS 675
Cdd:cd05042  80 GDLKAYLRSEREHERGDSDT--RTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTS---DLTVKIGDYGLAHSRYKED 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRALLPVKWMPPE-------AFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRgc 748
Cdd:cd05042 155 YIETDDKLWFPLRWTAPElvtefhdRLLVVDQTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVVREQDTKLPK-- 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 749 pgPV---------YRIMTQCWQhEPELRPSFASILERLQY 779
Cdd:cd05042 233 --PQlelpysdrwYEVLQFCWL-SPEQRPAAEDVHLLLTY 269
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
513-779 4.74e-45

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: 163.24  E-value: 4.74e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLV-IGLpgdsSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd05087   2 LKEIGHGWFGKVFLGEVnSGL----SSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHLGQ-PSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMARD 670
Cdd:cd05087  78 FCPLGDLKGYLRSCRAAESMaPDPLTLQ---RMACEVACGLLHLHRNNFVHSDLALRNCLLTA---DLTVKIGDYGLSHC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRASYYRRGDRALLPVKWMPPEA-------FLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd05087 152 KYKEDYFVTADQLWVPLRWIAPELvdevhgnLLVVDQTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTVREQQLK 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42544153 744 PPRG-CPGPV----YRIMTQCWQhEPELRPSFASILERLQY 779
Cdd:cd05087 232 LPKPqLKLSLaerwYEVMQFCWL-QPEQRPTAEEVHLLLSY 271
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
513-784 1.26e-44

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 163.31  E-value: 1.26e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIGlPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILlEL 592
Cdd:cd05110  12 VKVLGSGAFGTVYKGIWVP-EGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVT-QL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFGMARDIY 672
Cdd:cd05110  90 MPHGCLLDYVHEHKDNIGS------QLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVK--SPNHV-KITDFGLARLLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPV 752
Cdd:cd05110 161 GDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDV 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 753 YRIMTQCWQHEPELRPSFASILERLQYCTQDP 784
Cdd:cd05110 241 YMVMVKCWMIDADSRPKFKELAAEFSRMARDP 272
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
516-777 2.73e-44

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: 162.47  E-value: 2.73e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd05088  15 IGEGNFGQVLKARI---KKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRPHLGQP---------SPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDF 665
Cdd:cd05088  92 HGNLLDFLRKSRVLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDiyrASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPP 745
Cdd:cd05088 169 GLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKP 245
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 746 RGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05088 246 LNCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
516-777 3.99e-44

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: 158.59  E-value: 3.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd00180   1 LGKGSFGKVYKARDKE-----TGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLgqPSPLVMRdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRAS 675
Cdd:cd00180  76 GSLKDLLKENKGPL--SEEEALS----ILRQLLSALEYLHSNGIIHRDLKPENILLDSDG---TVKLADFGLAKDLDSDD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLgympypgrtnqevldfvvgggrmdpprgcpgpvYRI 755
Cdd:cd00180 147 SLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYELEEL---------------------------------KDL 193
                       250       260
                ....*....|....*....|..
gi 42544153 756 MTQCWQHEPELRPSFASILERL 777
Cdd:cd00180 194 IRRMLQYDPKKRPSAKELLEHL 215
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
507-784 1.82e-43

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 158.97  E-value: 1.82e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANVTLLRALGHGAFGEVYEGLVIGlPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPR 586
Cdd:cd05111   6 ETELRKLKVLGSGVFGTVHKGIWIP-EGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGgdmkSFLRHSRPHLGQPSPlvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFG 666
Cdd:cd05111  85 LVTQLLPLG----SLLDHVRQHRGSLGP---QLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLK--SPSQV-QVADFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPR 746
Cdd:cd05111 155 VADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQ 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 747 GCPGPVYRIMTQCWQHEPELRPSFASILERLQYCTQDP 784
Cdd:cd05111 235 ICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDP 272
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
511-775 1.09e-42

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 156.15  E-value: 1.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDK-----KTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    591 ELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARD 670
Cdd:smart00220  77 EYCEGGDLFDLLKKRGR-------LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD---EDGHVKLADFGLARQ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153    671 IYRASYYRR--GDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGR---MDPP 745
Cdd:smart00220 147 LDPGEKLTTfvGTPE-----YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKIGKPKppfPPPE 220
                          250       260       270
                   ....*....|....*....|....*....|
gi 42544153    746 RGCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:smart00220 221 WDISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
504-774 2.05e-42

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 159.79  E-value: 2.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLR 582
Cdd:cd05107  33 EMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLgPHLNIVNLLGACTK 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDM--------KSFLRH----SRP-----------------HLG----------------------- 610
Cdd:cd05107 113 GGPIYIITEYCRYGDLvdylhrnkHTFLQYyldkNRDdgslisggstplsqrksHVSlgsesdggymdmskdesadyvpm 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 611 ------------QPSP---------------------------LVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL 651
Cdd:cd05107 193 qdmkgtvkyadiESSNyespydqylpsapertrrdtlinespaLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLI 272
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 sCAGpsRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPG-RTNQ 730
Cdd:cd05107 273 -CEG--KLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPElPMNE 349
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 42544153 731 EVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd05107 350 QFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLV 393
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
513-778 2.98e-39

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: 147.35  E-value: 2.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVyeGLVIGLP-GDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL- 590
Cdd:cd05080   9 IRDLGEGHFGKV--SLYCYDPtNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGKSLQLi 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 -ELMSGGDMKSFLRHSRPHLGQpsplvmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMAR 669
Cdd:cd05080  87 mEYVPLGSLRDYLPKHSIGLAQ--------LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLD---NDRLVKIGDFGLAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRAS-YYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFS---------------LGymPYPGRTNQ-EV 732
Cdd:cd05080 156 AVPEGHeYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLThcdssqspptkflemIG--IAQGQMTVvRL 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 733 LDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05080 234 IELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILK 279
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
509-778 1.37e-38

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: 145.16  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEV----YEGLviglpGDSSPLQVAIKTLPElcSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd14205   5 HLKFLQQLGKGNFGSVemcrYDPL-----QDNTGEVVAVKKLQH--STEEHLrDFEREIEILKSLQHDNIVKYKGVCYSA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPR--LILLELMSGGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaK 661
Cdd:cd14205  78 GRRnlRLIMEYLPYGSLRDYLQKHKERIDH------IKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVE--NENRV-K 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYR-ASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLG---------YMPYPGRTNQ- 730
Cdd:cd14205 149 IGDFGLTKVLPQdKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIeksksppaeFMRMIGNDKQg 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42544153 731 -----EVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14205 229 qmivfHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVD 281
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
516-778 1.28e-36

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: 138.68  E-value: 1.28e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTL---PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLrATPRLIL-LE 591
Cdd:cd14061   2 IGVGGFGKVYRGIWRGE-------EVAVKAArqdPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCL-QPPNLCLvME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFL--RHSRPHLgqpsplvmrdLLQLAQDIAQGCHYLEENH---FIHRDIAARNCLLSCAGPS-----RVAK 661
Cdd:cd14061  74 YARGGALNRVLagRKIPPHV----------LVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENedlenKTLK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYR------ASYYrrgdrallpvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGrtnqevLDF 735
Cdd:cd14061 144 ITDFGLAREWHKttrmsaAGTY----------AWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKG------IDG 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 736 --VVGGGRMDP-----PRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14061 207 laVAYGVAVNKltlpiPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLE 256
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
511-769 4.67e-35

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: 134.25  E-value: 4.67e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGLPGDssplqVAIKTL-PELCSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14014   3 RLVRLLGRGGMGEVYRARDTLLGRP-----VAIKVLrPELAEDEEFReRFLREARALARLSHPNIVRVYDVGEDDGRPYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:cd14014  78 VMEYVEGGSLADLLR-------ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG---RVKLTDFGIA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDPPR-- 746
Cdd:cd14014 148 RALGDSGLTQTGSVLGTPA-YMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPPSPln 225
                       250       260
                ....*....|....*....|....
gi 42544153 747 -GCPGPVYRIMTQCWQHEPELRPS 769
Cdd:cd14014 226 pDVPPALDAIILRALAKDPEERPQ 249
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
516-777 5.55e-35

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: 134.39  E-value: 5.55e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTLPElcSPQDEL-----DFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd14146   2 IGVGGFGKVYRATWKGQ-------EVAVKAARQ--DPDEDIkataeSVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRphlGQPSPLVMRD-----LLQLAQDIAQGCHYLEENHF---IHRDIAARNCLL--------SCa 654
Cdd:cd14146  73 EFARGGTLNRALAAAN---AAPGPRRARRipphiLVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLlekiehddIC- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 655 gpSRVAKIGDFGMARDIYRASYYRrgdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLD 734
Cdd:cd14146 149 --NKTLKITDFGLAREWHRTTKMS----AAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAY 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 735 FVVGGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14146 222 GVAVNKLTLPiPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
516-783 5.90e-34

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: 131.02  E-value: 5.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTLPelcSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14058   1 VGRGSFGVVCKARWRNQ-------IVAVKIIE---SESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQgCHYLEENHFIHRDIAARNCLLSCAGpsRVAKIGDFGMARDIYRAS 675
Cdd:cd14058  71 GSLYNVLHGKEPKPIYTAAHAMSWALQCAKGVAY-LHSMKPKALIHRDLKPPNLLLTNGG--TVLKICDFGTACDISTHM 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLgYMPYP--GRTNQEVLDFVVGGGRMDPPRGCPGPVY 753
Cdd:cd14058 148 TNNKGSAA-----WMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDhiGGPAFRIMWAVHNGERPPLIKNCPKPIE 221
                       250       260       270
                ....*....|....*....|....*....|
gi 42544153 754 RIMTQCWQHEPELRPSFASILERLQYCTQD 783
Cdd:cd14058 222 SLMTRCWSKDPEKRPSMKEIVKIMSHLMQF 251
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
516-774 2.12e-33

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: 129.56  E-value: 2.12e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd06606   8 LGKGSFGSVYLALNL-----DTGELMAVKEVELSGDSEEELEALErEIRILSSLKHPNIVRYLGTERTENTLNIFLEYVP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHsrphLGQPSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIyRA 674
Cdd:cd06606  83 GGSLASLLKK----FGKLPEPVVR---KYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG---VVKLADFGCAKRL-AE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 675 SYYRRGDRALL--PVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDP--PRGCPG 750
Cdd:cd06606 152 IATGEGTKSLRgtPY-WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNPVAALFKIGSSGEPPpiPEHLSE 229
                       250       260
                ....*....|....*....|....
gi 42544153 751 PVYRIMTQCWQHEPELRPSfASIL 774
Cdd:cd06606 230 EAKDFLRKCLQRDPKKRPT-ADEL 252
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
516-778 2.68e-33

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: 130.01  E-value: 2.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEV----YEGLviglpGDSSPLQVAIKTLPElCSPQDELDFLMEALIISKFRHQNIVRCVGLSL---RATPRLI 588
Cdd:cd05081  12 LGKGNFGSVelcrYDPL-----GDNTGALVAVKQLQH-SGPDQQRDFQREIQILKALHSDFIVKYRGVSYgpgRRSLRLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LlELMSGGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagpSRV-AKIGDFGM 667
Cdd:cd05081  86 M-EYLPSGCLRDFLQRHRARLDA------SRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVE----SEAhVKIADFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 ARDIYR-ASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLG-----------YMPYPGRTNQEV--- 732
Cdd:cd05081 155 AKLLPLdKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCdkscspsaeflRMMGCERDVPALcrl 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 733 LDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05081 235 LELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLD 280
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
513-779 5.27e-33

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 128.83  E-value: 5.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVyegLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd05086   2 IQEIGNGWFGKV---LLGEIYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHSRPHLGQPSPLVMrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIY 672
Cdd:cd05086  79 CDLGDLKTYLANQQEKLRGDSQIML--LQRMACEIAAGLAHMHKHNFLHSDLALRNCYLT---SDLTVKVGDYGIGFSRY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASYYRRGDRALLPVKWMPPE---AFLEGIF----TSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPP 745
Cdd:cd05086 154 KEDYIETDDKKYAPLRWTAPElvtSFQDGLLaaeqTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVIKERQVKLF 233
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42544153 746 R-GCPGPV----YRIMTQCWQhEPELRPSFASILERLQY 779
Cdd:cd05086 234 KpHLEQPYsdrwYEVLQFCWL-SPEKRPTAEEVHRLLTY 271
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
513-778 6.40e-33

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: 128.89  E-value: 6.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVyEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLI--LL 590
Cdd:cd05079   9 IRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARD 670
Cdd:cd05079  88 EFLPSGSLKEYLPRNKNKIN------LKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGLTKA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IY-RASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFS---------------LGymPYPGR-TNQEVL 733
Cdd:cd05079 159 IEtDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspmtlflkmIG--PTHGQmTVTRLV 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 734 DFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd05079 237 RVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFE 281
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
516-777 1.39e-31

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: 124.14  E-value: 1.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglPGDSSPLQVaiktLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14065   1 LGKGFFGEVYKVT----HRETGKVMV----MKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLrhSRPHlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDI--YR 673
Cdd:cd14065  73 GTLEELL--KSMD----EQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMpdEK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRRGDRALL--PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIfsLGYMP----YPGRTNQEVLDfvVGGGRMDPPRG 747
Cdd:cd14065 147 TKKPDRKKRLTVvgSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI--IGRVPadpdYLPRTMDFGLD--VRAFRTLYVPD 222
                       250       260       270
                ....*....|....*....|....*....|
gi 42544153 748 CPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14065 223 CPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
516-778 3.17e-31

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: 123.17  E-value: 3.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTLPElcSPQDEL-----DFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd14148   2 IGVGGFGKVYKGLWRGE-------EVAVKAARQ--DPDEDIavtaeNVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSR--PHLgqpsplvmrdLLQLAQDIAQGCHYLEENHF---IHRDIAARNCLLSCAGP-----SRVA 660
Cdd:cd14148  73 EYARGGALNRALAGKKvpPHV----------LVNWAVQIARGMNYLHNEAIvpiIHRDLKSSNILILEPIEnddlsGKTL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYYRrgdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYpgrtnQEVLDFVVGGG 740
Cdd:cd14148 143 KITDFGLAREWHKTTKMS----AAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPY-----REIDALAVAYG 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 741 ------RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14148 213 vamnklTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLE 256
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
511-777 3.59e-31

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 122.97  E-value: 3.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGlVIGLPGDSSPLQVAIkTLPELCSPQDELD--FLMEALIISKFRHQNIVRCVGLSLRAtPRLI 588
Cdd:cd05037   2 TFHEHLGQGTFTNIYDG-ILREVGDGRVQEVEV-LLKVLDSDHRDISesFFETASLMSQISHKHLVKLYGVCVAD-ENIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL---SCAGPSRVAKIGDF 665
Cdd:cd05037  79 VQEYVRYGPLDKYLRR------MGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLareGLDGYPPFIKLSDP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRASYyrrgdrALLPVKWMPPEAFLEGI--FTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd05037 153 GVPITVLSREE------RVDRIPWIAPECLRNLQanLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLP 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 42544153 744 PPRGcpGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05037 227 APDC--AELAELIMQCWTYEPTKRPSFRAILRDL 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
516-777 6.63e-31

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: 122.56  E-value: 6.63e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGdssplQVAIKTLPELCSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFG-----MVAIKCLHSSPNCIEERkALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHsrphLGQPSPLVMRdlLQLAQDIAQGCHYLE--ENHFIHRDIAARNCLLScagPSRVAKIGDFGMARdIY 672
Cdd:cd13978  76 NGSLKSLLER----EIQDVPWSLR--FRIIHEIALGMNFLHnmDPPLLHHDLKPENILLD---NHFHVKISDFGLSK-LG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASY--YRRGDRALL--PVKWMPPEAFLEGI--FTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGG------ 740
Cdd:cd13978 146 MKSIsaNRRRGTENLggTPIYMAPEAFDDFNkkPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLIMQIVSKGdrpsld 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 741 ---RMDPPRGCPGPVyRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd13978 225 digRLKQIENVQELI-SLMIRCWDGNPDARPTFLECLDRL 263
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
516-778 1.43e-30

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 121.61  E-value: 1.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglpgdSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14066   1 IGSGGFGTVYKGVL------ENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPhlGQPSPLVMRdlLQLAQDIAQGCHYLEE---NHFIHRDIAARNCLLScagPSRVAKIGDFGMARDI- 671
Cdd:cd14066  75 GSLEDRLHCHKG--SPPLPWPQR--LKIAKGIARGLEYLHEecpPPIIHGDIKSSNILLD---EDFEPKLTDFGLARLIp 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYYRRGD-RALLPvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMP-YPGRTNQEVLDFV-----VGGGR--- 741
Cdd:cd14066 148 PSESVSKTSAvKGTIG--YLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAvDENRENASRKDLVewvesKGKEEled 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 742 -MDP-PRGCPGP-------VYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14066 225 iLDKrLVDDDGVeeeeveaLLRLALLCTRSDPSLRPSMKEVVQMLE 270
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
504-777 2.63e-30

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: 120.92  E-value: 2.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGLpgdssplQVAIKTL---PELCSPQDELDFLMEALIISKFRHQNIVRCVGLS 580
Cdd:cd14145   2 EIDFSELVLEEIIGIGGFGKVYRAIWIGD-------EVAVKAArhdPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 581 LRATPRLILLELMSGGDMKSFLRHSR--PHLgqpsplvmrdLLQLAQDIAQGCHYLEENHF---IHRDIAARNCLL---- 651
Cdd:cd14145  75 LKEPNLCLVMEFARGGPLNRVLSGKRipPDI----------LVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILIlekv 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 -SCAGPSRVAKIGDFGMARDIYRASYYRrgdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQ 730
Cdd:cd14145 145 eNGDLSNKILKITDFGLAREWHRTTKMS----AAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGL 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42544153 731 EVLDFVVGGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14145 220 AVAYGVAMNKLSLPiPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQL 267
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
511-847 4.77e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 125.13  E-value: 4.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGLPgdsspLQVAIKTL-PELCSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:COG0515  10 RILRLLGRGGMGVVYLARDLRLG-----RPVALKVLrPELAADPEARErFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:COG0515  85 VMEYVEGESLADLLRRRGP-------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG---RVKLIDFGIA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDPPR-- 746
Cdd:COG0515 155 RALGGATLTQTGTVVGTPG-YMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSElr 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 747 -GCPGPVYRIMTQCWQHEPELRP-SFASILERLQYCTQDPDVLNSLLPMELGPTPEEEGTSGLGNRSLECLRPPQPQELS 824
Cdd:COG0515 233 pDLPPALDAIVLRALAKDPEERYqSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 312
                       330       340
                ....*....|....*....|...
gi 42544153 825 PEKLKSWGGSPLGPWLSSGLKPL 847
Cdd:COG0515 313 AAAAAAAAAAPAAAAAAAAAAAA 335
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
510-778 4.95e-29

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: 117.05  E-value: 4.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGLpgdssplQVAIKTLPElcSPQDELDFL-----MEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd14147   5 LRLEEVIGIGGFGKVYRGSWRGE-------LVAVKAARQ--DPDEDISVTaesvrQEARLFAMLAHPNIIALKAVCLEEP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSR--PHLgqpsplvmrdLLQLAQDIAQGCHYLEENHF---IHRDIAARNCLLSCAGPS-- 657
Cdd:cd14147  76 NLCLVMEYAAGGPLSRALAGRRvpPHV----------LVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIENdd 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 ---RVAKIGDFGMARDIYRASYYRrgdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLD 734
Cdd:cd14147 146 mehKTLKITDFGLAREWHKTTQMS----AAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAY 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 735 FVVGGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14147 221 GVAVNKLTLPiPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLE 265
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
517-778 2.44e-28

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: 114.28  E-value: 2.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 517 GHGAFGEVYEGlvIGLPGDSsplQVAIKTLpelcspqdeLDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGG 596
Cdd:cd14060   2 GGGSFGSVYRA--IWVSQDK---EVAVKKL---------LKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 597 DMKSFLRHSRPHlgqpsPLVMRDLLQLAQDIAQGCHYLEEN---HFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYR 673
Cdd:cd14060  68 SLFDYLNSNESE-----EMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADG---VLKICDFGASRFHSH 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRRgdRALLPvkWMPPEaFLEGIFTSKT-DSWSFGVLLWEIFSLgYMPYPGRTNQEVLDFVVGGG-RMDPPRGCPGP 751
Cdd:cd14060 140 TTHMSL--VGTFP--WMAPE-VIQSLPVSETcDTYSYGVVLWEMLTR-EVPFKGLEGLQVAWLVVEKNeRPTIPSSCPRS 213
                       250       260
                ....*....|....*....|....*..
gi 42544153 752 VYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14060 214 FAELMRRCWEADVKERPSFKQIIGILE 240
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
514-778 3.42e-28

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: 115.29  E-value: 3.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgdsSPLQVAIKTLPEL--CSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd14158  21 NKLGEGGFGVVFKGYI-------NDKNVAVKKLAAMvdISTEDLTKqFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLrhsrPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARD 670
Cdd:cd14158  94 TYMPNGSLLDRL----ACLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLD---ETFVPKISDFGLARA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRASYYRRGDRALLPVKWMPPEAfLEGIFTSKTDSWSFGVLLWEIFSlGYMPY-PGRTNQEVL--------------DF 735
Cdd:cd14158 167 SEKFSQTIMTERIVGTTAYMAPEA-LRGEITPKSDIFSFGVVLLEIIT-GLPPVdENRDPQLLLdikeeiedeektieDY 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 736 V-VGGGRMDPPRgcPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14158 245 VdKKMGDWDSTS--IEAMYSVASQCLNDKKNRRPDIAKVQQLLQ 286
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
516-777 5.56e-27

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: 110.28  E-value: 5.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTLPElcspQDELDFLMealiISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14059   1 LGSGAQGAVFLGKFRGE-------EVAVKKVRD----EKETDIKH----LRKLNHPNIIKFKGVCTQAPCYCILMEYCPY 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLgqPSPLVmrdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagpSRVAKIGDFGMARDIyras 675
Cdd:cd14059  66 GQLYEVLRAGREIT--PSLLV-----DWSKQIASGMNYLHLHKIIHRDLKSPNVLVTY---NDVLKISDFGTSKEL---- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 yyrrGDRALL-----PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLdFVVGGG--RMDPPRGC 748
Cdd:cd14059 132 ----SEKSTKmsfagTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAII-WGVGSNslQLPVPSTC 205
                       250       260
                ....*....|....*....|....*....
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14059 206 PDGFKLLMKQCWNSKPRNRPSFRQILMHL 234
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
496-778 1.33e-26

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: 110.15  E-value: 1.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 496 WPLPPGvtevspaNVTLLRALGHGAFGEVYEGLVIGlpgdssplQVAIKTLPELC-SPQDELDFLMEALIISKFRHQNIV 574
Cdd:cd14151   3 WEIPDG-------QITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNIL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 575 RCVGLSLRatPRL-ILLELMSGGDMKSFLRHSRphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSc 653
Cdd:cd14151  68 LFMGYSTK--PQLaIVTQWCEGSSLYHHLHIIE------TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 654 agPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQ 730
Cdd:cd14151 139 --EDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNR 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42544153 731 EVLDFVVGGGRMDPP-----RGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14151 216 DQIIFMVGRGYLSPDlskvrSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 268
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
516-778 1.52e-26

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: 109.41  E-value: 1.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlpgdssplQVAIKTL----PelcSPQDELDFLMEALIISKFRHQNIVRCVGLSLRatPRL-ILL 590
Cdd:cd14062   1 IGSGSFGTVYKGRWHG--------DVAVKKLnvtdP---TPSQLQAFKNEVAVLRKTRHVNILLFMGYMTK--PQLaIVT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGgdmKSFLRHSrpHLgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARD 670
Cdd:cd14062  68 QWCEG---SSLYKHL--HV-LETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLH---EDLTVKIGDFGLATV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRASYYRRGDRALLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDPPRG 747
Cdd:cd14062 139 KTRWSGSQQFEQPTGSILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQILFMVGRGYLRPDLS 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 748 -----CPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14062 218 kvrsdTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
516-775 1.83e-26

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 109.24  E-value: 1.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd06627   8 IGRGAFGSVYKGLNL-----NTGEFVAIKQISLEKIPKSDLKSVMgEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRhsrPHLGQPSPLVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRA 674
Cdd:cd06627  83 NGSLASIIK---KFGKFPESLVAVYIYQ----VLEGLAYLHEQGVIHRDIKGANILTTKDG---LVKLADFGVATKLNEV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 675 SyyrrgDRALLPV---KWMPPEAF-LEGIfTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPG 750
Cdd:cd06627 153 E-----KDENSVVgtpYWMAPEVIeMSGV-TTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDDHPPLPENISP 225
                       250       260
                ....*....|....*....|....*
gi 42544153 751 PVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06627 226 ELRDFLLQCFQKDPTLRPSAKELLK 250
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
510-769 5.02e-26

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: 108.06  E-value: 5.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLViglpgDSSPLQVAIKTLPeLCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARH-----KKTGQIVAIKKIN-LESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHsRPHLGQPSPL--VMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFG- 666
Cdd:cd05122  76 MEFCSGGSLKDLLKN-TNKTLTEQQIayVCKEVLK-------GLEYLHSHGIIHRDIKAANILLTSDG---EVKLIDFGl 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 ---MARDIYRASYYrrGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVVgggrMD 743
Cdd:cd05122 145 saqLSDGKTRNTFV--GTPY-----WMAPEVIQGKPYGFKADIWSLGITAIEMA-EGKPPYSELPPMKALFLIA----TN 212
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 744 PPRGCPGPVYR------IMTQCWQHEPELRPS 769
Cdd:cd05122 213 GPPGLRNPKKWskefkdFLKKCLQKDPEKRPT 244
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
510-778 2.18e-25

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: 106.64  E-value: 2.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGlpgdssplQVAIKTLpELCSPQDEL--DFLMEALIISKFRHQNIVRCVGLSLRatPRL 587
Cdd:cd14150   2 VSMLKRIGTGSFGTVFRGKWHG--------DVAVKIL-KVTEPTPEQlqAFKNEMQVLRKTRHVNILLFMGFMTR--PNF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGdmKSFLRHSrpHLGQPSPLVMRdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGM 667
Cdd:cd14150  71 AIITQWCEG--SSLYRHL--HVTETRFDTMQ-LIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLH---EGLTVKIGDFGL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 ARDIYRASYYRRGDRALLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDP 744
Cdd:cd14150 143 ATVKTRWSGSQQVEQPSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDQIIFMVGRGYLSP 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42544153 745 -----PRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14150 222 dlsklSSNCPKAMKRLLIDCLKFKREERPLFPQILVSIE 260
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
554-778 3.85e-25

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: 105.29  E-value: 3.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 554 DELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHsrphlgQPSPLVMRDLLQLAQDIAQGCHY 633
Cdd:cd14156  31 DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAR------EELPLSWREKVELACDISRGMVY 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 634 LEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASyYRRGDRALLPVK---WMPPEAFLEGIFTSKTDSWSFG 710
Cdd:cd14156 105 LHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVGEMP-ANDPERKLSLVGsafWMAPEMLRGEPYDRKVDVFSFG 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 711 VLLWEIfsLGYMP-----YPgRTNQEVLDFVVGGGRMDpprGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14156 184 IVLCEI--LARIPadpevLP-RTGDFGLDVQAFKEMVP---GCPEPFLDLAASCCRMDAFKRPSFAELLDELE 250
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
516-778 3.56e-23

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: 99.86  E-value: 3.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYE------GLVIGLPGDSSPLQVAiktlpelcspqdelDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd14155   1 IGSGFFSEVYKvrhrtsGQVMALKMNTLSSNRA--------------NMLREVQLMNRLSHPNILRFMGVCVHQGQLHAL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLrHSRPHLGQPSPLvmrdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMAR 669
Cdd:cd14155  67 TEYINGGNLEQLL-DSNEPLSWTVRV------KLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRASYyrRGDRalLPV----KWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL-----GYMPypgRTNQEVLDF----- 735
Cdd:cd14155 140 KIPDYSD--GKEK--LAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARiqadpDYLP---RTEDFGLDYdafqh 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42544153 736 VVGggrmdpprGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14155 213 MVG--------DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLE 247
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
504-778 6.67e-23

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: 99.72  E-value: 6.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIGlpgdssplQVAIKTLPEL-CSPQDELDFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd14149   8 EIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVdPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATpRLILLELMSGGDMKSFLrhsrpHLgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKI 662
Cdd:cd14149  80 DN-LAIVTQWCEGSSLYKHL-----HV-QETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd14149 150 GDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRDQIIFMVGR 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 740 GRMDPP-----RGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14149 229 GYASPDlsklyKNCPKAMKRLVADCIKKVKEERPLFPQILSSIE 272
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
514-774 1.11e-22

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 98.76  E-value: 1.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLviglpGDSSPLQVAIKTLpELCSPQDELD----FLMEAL-----IISKFRHQNIVRCVGLSLRAT 584
Cdd:cd06628   6 ALIGSGSFGSVYLGM-----NASSGELMAVKQV-ELPSVSAENKdrkkSMLDALqreiaLLRELQHENIVQYLGSSSDAN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHsrpHLGQPSPLVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGD 664
Cdd:cd06628  80 HLNIFLEYVPGGSVATLLNN---YGAFEESLVRNFVRQ----ILKGLNYLHNRGIIHRDIKGANILVDNKG---GIKISD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDI--YRASYYRRGDRALL--PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLdFVVGG- 739
Cdd:cd06628 150 FGISKKLeaNSLSTKNNGARPSLqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAI-FKIGEn 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 740 GRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd06628 228 ASPTIPSNISSEARDFLEKTFEIDHNKRPTADELL 262
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
516-780 1.87e-22

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: 97.60  E-value: 1.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL-ILLEL 592
Cdd:cd14064   1 IGSGSFGKVYKGRCRNK-------IVAIKRYraNTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFaIVTQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRhsrphlGQPSPLVMRDLLQLAQDIAQGCHYLEE--NHFIHRDIAARNCLLSCAGPSRVAkigDFGMARD 670
Cdd:cd14064  74 VSGGSLFSLLH------EQKRVIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVA---DFGESRF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRasyyrRGDRALLP----VKWMPPEAFLE-GIFTSKTDSWSFGVLLWEIFSlGYMPYPG-RTNQEVLDFVVGGGRMDP 744
Cdd:cd14064 145 LQS-----LDEDNMTKqpgnLRWMAPEVFTQcTRYSIKADVFSYALCLWELLT-GEIPFAHlKPAAAAADMAYHHIRPPI 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 745 PRGCPGPVYRIMTQCWQHEPELRPSFASILERLQYC 780
Cdd:cd14064 219 GYSIPKPISSLLMRGWNAEPESRPSFVEIVALLEPC 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
516-750 4.07e-22

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: 96.52  E-value: 4.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEG--LVIGLPgdssplqVAIKTL------PELcspQDELDflMEALIISKFRHQNIVRCvgLSLRATPRL 587
Cdd:cd14009   1 IGRGSFATVWKGrhKQTGEV-------VAIKEIsrkklnKKL---QENLE--SEIAILKSIKHPNIVRL--YDVQKTEDF 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 I--LLELMSGGDMKSFLRHsrpHLGQPSPLVMRDLLQLAQdiaqGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDF 665
Cdd:cd14009  67 IylVLEYCAGGDLSQYIRK---RGRLPEAVARHFMQQLAS----GLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADF 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRASY---------YrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFV 736
Cdd:cd14009 140 GFARSLQPASMaetlcgsplY------------MAPEILQFQKYDAKADLWSVGAILFEML-VGKPPFRGSNHVQLLRNI 206
                       250
                ....*....|....
gi 42544153 737 VGGGRMDPPRGCPG 750
Cdd:cd14009 207 ERSDAVIPFPIAAQ 220
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
512-775 7.13e-22

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: 96.27  E-value: 7.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpgdssPLQ--VAIKTLpELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd06610   5 LIEVIGSGATAVVYAAYCL-------PKKekVAIKRI-DLEKCQTSMDELRkEIQAMSQCNHPNVVSYYTSFVVGDELWL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPHLGQPSPL---VMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDF 665
Cdd:cd06610  77 VMPLLSGGSLLDIMKSSYPRGGLDEAIiatVLKEVLK-------GLEYLHSNGQIHRDVKAGNILLGEDGS---VKIADF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMArdiyrASYYRRGDRALLPVK-------WMPPEAFLEGI-FTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVLDFVV 737
Cdd:cd06610 147 GVS-----ASLATGGDRTRKVRKtfvgtpcWMAPEVMEQVRgYDFKADIWSFGITAIEL-ATGAAPYSKYPPMKVLMLTL 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 738 GGgrmDPPR-------GCPGPVYRIM-TQCWQHEPELRPSFASILE 775
Cdd:cd06610 221 QN---DPPSletgadyKKYSKSFRKMiSLCLQKDPSKRPTAEELLK 263
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
516-778 7.69e-22

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: 96.26  E-value: 7.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlpgdssplQVAIKTLPELCSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRAtPRL-ILLELM 593
Cdd:cd14063   8 IGKGRFGRVHRGRWHG--------DVAIKLLNIDYLNEEQLEaFKEEVAAYKNTRHDNLVLFMGACMDP-PHLaIVTSLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLRHSRphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAkIGDFGMARdIYR 673
Cdd:cd14063  79 KGRTLYSLIHERK------EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE---NGRVV-ITDFGLFS-LSG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRRGDRAL-LPVKWMP---PE------AFLEGI----FTSKTDSWSFGVLLWEIFSlGYMPYpGRTNQEVLDFVVGG 739
Cdd:cd14063 148 LLQPGRREDTLvIPNGWLCylaPEiiralsPDLDFEeslpFTKASDVYAFGTVWYELLA-GRWPF-KEQPAESIIWQVGC 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 740 GrMDPPR---GCPGPVYRIMTQCWQHEPELRPSFA---SILERLQ 778
Cdd:cd14063 226 G-KKQSLsqlDIGREVKDILMQCWAYDPEKRPTFSdllRMLERLP 269
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
509-775 9.52e-21

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: 92.58  E-value: 9.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLP-ELCSPQDELDFLMEALIISKFRHQNIVRCvgLSLRATPRL 587
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHK-----LTGEKVAIKIIDkSKLKEEIEEKIKREIEIMKLLNHPNIIKL--YEVIETENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILL--ELMSGGDMKSFLRHSRPhlgqpsplvmrdllqLAQDIAQ--------GCHYLEENHFIHRDIAARNCLLSCAGps 657
Cdd:cd14003  74 IYLvmEYASGGELFDYIVNNGR---------------LSEDEARrffqqlisAVDYCHSNGIVHRDLKLENILLDKNG-- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 rVAKIGDFGMARdiyrasYYRRGDRALLPV---KWMPPEAFL-EGIFTSKTDSWSFGVLLweiFSL--GYMPYPGRTNQE 731
Cdd:cd14003 137 -NLKIIDFGLSN------EFRGGSLLKTFCgtpAYAAPEVLLgRKYDGPKADVWSLGVIL---YAMltGYLPFDDDNDSK 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 732 VLDFVVGGGRMDPPRGCPGPVyRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14003 207 LFRKILKGKYPIPSHLSPDAR-DLIRRMLVVDPSKRITIEEILN 249
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
512-774 9.68e-21

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: 92.87  E-value: 9.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYegLVIGLPGDSsplQVAIKTLPEL----CSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL 587
Cdd:cd08222   4 VVRKLGSGNFGTVY--LVSDLKATA---DEELKVLKEIsvgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRPHLGQPSP-LVMRDLLQLAQdiaqGCHYLEENHFIHRDIAARNCLLScagpSRVAKIGDFG 666
Cdd:cd08222  79 IVTEYCEGGDLDDKISEYKKSGTTIDEnQILDWFIQLLL----AVQYMHERRILHRDLKAKNIFLK----NNVIKVGDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRAS----------YYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYmPYPGRTNQEVLDFV 736
Cdd:cd08222 151 ISRILMGTSdlattftgtpYY------------MSPEVLKHEGYNSKSDIWSLGCILYEMCCLKH-AFDGQNLLSVMYKI 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 737 VGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd08222 218 VEGETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEIL 255
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
516-778 1.94e-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: 92.19  E-value: 1.94e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVyeglviglpgdsspLQVAIKT------LPELCSPQDEL--DFLMEALIISKFRHQNIVRCVGLSLRATPRL 587
Cdd:cd14154   1 LGKGFFGQA--------------IKVTHREtgevmvMKELIRFDEEAqrNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLN 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHsrphLGQPSPLVMRdlLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGM 667
Cdd:cd14154  67 LITEYIPGGTLKDVLKD----MARPLPWAQR--VRFAKDIASGMAYLHSMNIIHRDLNSHNCLVR---EDKTVVVADFGL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 ARDI------YRASYYRRGDRALLPVK------------WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL-----GYMPy 724
Cdd:cd14154 138 ARLIveerlpSGNMSPSETLRHLKSPDrkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRveadpDYLP- 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42544153 725 pgRTNQEVLDfvVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14154 217 --RTKDFGLN--VDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLE 266
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
513-791 1.97e-20

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: 92.15  E-value: 1.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLpELCSPQDEL-DFLMEALIISKFRH---QNIVRCVGLSLRATPRLI 588
Cdd:cd06917   6 LELVGRGSYGAVYRGYHV-----KTGRVVALKVL-NLDTDDDDVsDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRH---SRPHLGqpspLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGpsRVaKIGDF 665
Cdd:cd06917  80 IMDYCEGGSIRTLMRAgpiAERYIA----VIMREVLV-------ALKFIHKDGIIHRDIKAANILVTNTG--NV-KLCDF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRASyYRRGDRALLPVkWMPPEAFLEGI-FTSKTDSWSFGVLLWEIfSLGYMPYPGrtnQEVLDFVVGGGRMDP 744
Cdd:cd06917 146 GVAASLNQNS-SKRSTFVGTPY-WMAPEVITEGKyYDTKADIWSLGITTYEM-ATGNPPYSD---VDALRAVMLIPKSKP 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544153 745 PRgCPGPVYRIMTQ-----CWQHEPELRPSfASILERLQYCTQDPDVLNSLL 791
Cdd:cd06917 220 PR-LEGNGYSPLLKefvaaCLDEEPKDRLS-ADELLKSKWIKQHSKTPTSVL 269
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
511-776 1.97e-20

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: 91.76  E-value: 1.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYegLVIGLPGDSsplQVAIKTLP-ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd08215   3 EKIRVIGKGSFGSAY--LVRRKSDGK---LYVLKEIDlSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRpHLGQPSP--LVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGM 667
Cdd:cd08215  78 MEYADGGDLAQKIKKQK-KKGQPFPeeQILDWFVQ----ICLALKYLHSRKILHRDLKTQNIFLTKDG---VVKLGDFGI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 AR----DIYRAS------YYrrgdrallpvkwMPPEAFlEGI-FTSKTDSWSFGVLLWEIFSLGYmPYPGRTNQEVLDFV 736
Cdd:cd08215 150 SKvlesTTDLAKtvvgtpYY------------LSPELC-ENKpYNYKSDIWALGCVLYELCTLKH-PFEANNLPALVYKI 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 737 VGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILER 776
Cdd:cd08215 216 VKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSANEILSS 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
512-775 5.64e-20

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: 90.73  E-value: 5.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd06623   5 RVKVLGQGSSGVVYKVRHKP-----TGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRhSRPHLGQPsplvmrDLLQLAQDIAQGCHYL-EENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARD 670
Cdd:cd06623  80 YMDGGSLADLLK-KVGKIPEP------VLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKG---EVKIADFGISKV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRASYYRR---GDrallpVKWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPY--PGRTNQ-EVLDFVVGGGRMDP 744
Cdd:cd06623 150 LENTLDQCNtfvGT-----VTYMSPERIQGESYSYAADIWSLGLTLLE-CALGKFPFlpPGQPSFfELMQAICDGPPPSL 223
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 745 PRGCPGPVYR-IMTQCWQHEPELRPSFASILE 775
Cdd:cd06623 224 PAEEFSPEFRdFISACLQKDPKKRPSAAELLQ 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
512-775 7.77e-20

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: 89.84  E-value: 7.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYegLVIGLpgdSSPLQVAIKTLP--ELCSPQDELDFLMEALIISKFRHQNIVRCVGlSLRATPRLIL 589
Cdd:cd14007   4 IGKPLGKGKFGNVY--LAREK---KSGFIVALKVISksQLQKSGLEHQLRREIEIQSHLRHPNILRLYG-YFEDKKRIYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 -LELMSGGDMKSFLRhSRPHLgqPSPLVMRDLLQLAQDIaqgcHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:cd14007  78 iLEYAPNGELYKELK-KQKRF--DEKEAAKYIYQLALAL----DYLHSKNIIHRDIKPENILLGSNG---ELKLADFGWS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDiyrASYYRRG------DrallpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVgggRM 742
Cdd:cd14007 148 VH---APSNRRKtfcgtlD-------YLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQETYKRIQ---NV 213
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 743 DPPRgcPGPVYRI----MTQCWQHEPELRPSFASILE 775
Cdd:cd14007 214 DIKF--PSSVSPEakdlISKLLQKDPSKRLSLEQVLN 248
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
509-776 1.47e-19

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: 89.25  E-value: 1.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGlviglPGDSSPLQVAIKTLPELCSPQDELDFLM-EALIISKFRHQNIVRCVGlSLRATPRL 587
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLA-----KAKSDSEHCVIKEIDLTKMPVKEKEASKkEVILLAKMKHPNIVTFFA-SFQENGRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 -ILLELMSGGD-MKSFLRhsrphlgQPSPLVMRD-LLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsRVAKIGD 664
Cdd:cd08225  75 fIVMEYCDGGDlMKRINR-------QRGVLFSEDqILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNG--MVAKLGD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRASYYRRgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYmPYPGRTNQEVLdFVVGGGRMDP 744
Cdd:cd08225 146 FGIARQLNDSMELAY--TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKH-PFEGNNLHQLV-LKICQGYFAP 221
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 745 PRgcPGPVY---RIMTQCWQHEPELRPSFASILER 776
Cdd:cd08225 222 IS--PNFSRdlrSLISQLFKVSPRDRPSITSILKR 254
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
511-775 1.59e-19

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: 89.73  E-value: 1.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLpELCSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd06642   7 TKLERIGKGSFGEVYKGI-----DNRTKEVVAIKII-DLEEAEDEIeDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRhsrphlgqPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMAR 669
Cdd:cd06642  81 MEYLGGGSALDLLK--------PGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD---VKLADFGVAG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVLDFVvgggrmdpPRGCP 749
Cdd:cd06642 150 QL-TDTQIKRNTFVGTPF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLI--------PKNSP 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 42544153 750 --------GPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06642 219 ptlegqhsKPFKEFVEACLNKDPRFRPTAKELLK 252
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
516-773 1.15e-18

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: 86.92  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVyeglvIGLPGDSSPLQVAIKTLPElCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14222   1 LGKGFFGQA-----IKVTHKATGKVMVMKELIR-CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQPSplvmrdlLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAkigDFGMARDIY--- 672
Cdd:cd14222  75 GTLKDFLRADDPFPWQQK-------VSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVA---DFGLSRLIVeek 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 ----------RASYYRRGDR-----ALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGY-----MPypgRTnqev 732
Cdd:cd14222 145 kkpppdkpttKKRTLRKNDRkkrytVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYadpdcLP---RT---- 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 733 LDF---VVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASI 773
Cdd:cd14222 218 LDFglnVRLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPAFSKL 261
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
513-775 1.52e-18

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: 86.66  E-value: 1.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLviglpgDSSPLQVAIKTLPELCSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd06641   9 LEKIGKGSFGEVFKGI------DNRTQKVVAIKIIDLEEAEDEIeDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLrhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDI 671
Cdd:cd06641  83 YLGGGSALDLL--------EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE---VKLADFGVAGQL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 yRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVLDFVvggGRMDPPR---GC 748
Cdd:cd06641 152 -TDTQIKRN*FVGTPF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLI---PKNNPPTlegNY 225
                       250       260
                ....*....|....*....|....*..
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06641 226 SKPLKEFVEACLNKEPSFRPTAKELLK 252
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
510-777 2.08e-18

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 86.12  E-value: 2.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEG--LVIG------------LPGDSSPLQVAIKTLPElcSPQD-ELDFLMEALIISKFRHQNIV 574
Cdd:cd05076   1 ITQLSHLGQGTRTNIYEGrlLVEGsgepeedkelvpGRDRGQELRVVLKVLDP--SHHDiALAFFETASLMSQVSHTHLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 575 RCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVmrdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLS-- 652
Cdd:cd05076  79 FVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKGHVPMAWKFV------VARQLASALSYLENKNLVHGNVCAKNILLArl 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 653 --CAGPSRVAKIGDFGMARDIYraSYYRRGDRallpVKWMPPEAFLEGI-FTSKTDSWSFGVLLWEIFSLGYMPYPGRTN 729
Cdd:cd05076 153 glEEGTSPFIKLSDPGVGLGVL--SREERVER----IPWIAPECVPGGNsLSTAADKWGFGATLLEICFNGEAPLQSRTP 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42544153 730 QEVLDFVVGGGRMDPPrGCPgPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05076 227 SEKERFYQRQHRLPEP-SCP-ELATLISQCLTYEPTQRPSFRTILRDL 272
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
509-774 2.12e-18

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: 85.91  E-value: 2.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELcSPQDELDFLMEALIISKFRHQNIVR-----CVGLSLra 583
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLS---DNQVYALKEVNLGSL-SQKEREDSVNEIRLLASVNHPNIIRykeafLDGNRL-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 tprLILLELMSGGDMKSFLRHSRpHLGQPSP--LVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAK 661
Cdd:cd08530  75 ---CIVMEYAPFGDLSKLISKRK-KKRRLFPedDIWRIFIQ----MLRGLKALHDQKILHRDLKSANILLSAGD---LVK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRASYYRRGDRALlpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYmPYPGRTNQEvLDFVVGGGR 741
Cdd:cd08530 144 IGDLGISKVLKKNLAKTQIGTPL----YAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRP-PFEARTMQE-LRYKVCRGK 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 742 MDPPRgcpgPVY-----RIMTQCWQHEPELRPSFASIL 774
Cdd:cd08530 218 FPPIP----PVYsqdlqQIIRSLLQVNPKKRPSCDKLL 251
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
513-777 2.67e-18

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 85.77  E-value: 2.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGL--VIGLPGDSSPLQVAIKTLPELCSPQDElDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd05078   4 NESLGQGTFTKIFKGIrrEVGDYGQLHETEVLLKVLDKAHRNYSE-SFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS-----CAGPSRVAKIGDF 665
Cdd:cd05078  83 EYVKFGSLDTYLKKNK------NCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIreedrKTGNPPFIKLSDP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMA-----RDIYrasyyrrgdraLLPVKWMPPEAFLEGI-FTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd05078 157 GISitvlpKDIL-----------LERIPWVPPECIENPKnLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDR 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 740 GRMDPPRGCpgPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd05078 226 HQLPAPKWT--ELANLINNCMDYEPDHRPSFRAIIRDL 261
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
516-775 3.52e-18

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: 85.30  E-value: 3.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglpgDSSPLQ-VAIKTL--PELC----------SPQDELDFLM-EALIISKFRHQNIVRCV---- 577
Cdd:cd14008   1 LGRGSFGKVKLAL------DTETGQlYAIKIFnkSRLRkrregkndrgKIKNALDDVRrEIAIMKKLDHPNIVRLYevid 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 578 ---GLSLratprLILLELMSGGDMKSflrhsRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSca 654
Cdd:cd14008  75 dpeSDKL-----YLVLEYCEGGPVME-----LDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLT-- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 655 gPSRVAKIGDFGMARdiyrasYYRRGDRALLPVK----WMPPEAFLEGIFT---SKTDSWSFGVLLWeIFSLGYMPYPGR 727
Cdd:cd14008 143 -ADGTVKISDFGVSE------MFEDGNDTLQKTAgtpaFLAPELCDGDSKTysgKAADIWALGVTLY-CLVFGRLPFNGD 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42544153 728 TNQEVLDFVVGGGRMDPPRGCPGPVYR-IMTQCWQHEPELRPSFASILE 775
Cdd:cd14008 215 NILELYEAIQNQNDEFPIPPELSPELKdLLRRMLEKDPEKRITLKEIKE 263
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
511-769 4.03e-18

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: 85.37  E-value: 4.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLviglpgDSSPLQ-VAIKTLpELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd06609   4 TLLERIGKGSFGEVYKGI------DKRTNQvVAIKVI-DLEEAEDEIEDIQqEIQFLSQCDSPYITKYYGSFLKGSKLWI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPHLGQPSpLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPSRVAkigDFGMA 668
Cdd:cd06609  77 IMEYCGGGSVLDLLKPGPLDETYIA-FILREVLL-------GLEYLHSEGKIHRDIKAANILLSEEGDVKLA---DFGVS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLdFVVggGRMDPPRgC 748
Cdd:cd06609 146 GQL-TSTMSKRNTFVGTPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVL-FLI--PKNNPPS-L 218
                       250       260
                ....*....|....*....|....*.
gi 42544153 749 PGPVYR-----IMTQCWQHEPELRPS 769
Cdd:cd06609 219 EGNKFSkpfkdFVELCLNKDPKERPS 244
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
512-777 5.44e-18

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: 84.74  E-value: 5.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGLpgdssplQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPR---LI 588
Cdd:cd13979   7 LQEPLGSGGFGSVYKATYKGE-------TVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAETGTDFAslgLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPhlgqpsPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMA 668
Cdd:cd13979  80 IMEYCGNGTLQQLIYEGSE------PLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIS---EQGVCKLCDFGCS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 ------RDIYRASYYRRGDrallpVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGrTNQEVLDFVVGGG-R 741
Cdd:cd13979 151 vklgegNEVGTPRSHIGGT-----YTYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAG-LRQHVLYAVVAKDlR 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42544153 742 MDPPRGC---PGPVYR-IMTQCWQHEPELRPS-FASILERL 777
Cdd:cd13979 224 PDLSGLEdseFGQRLRsLISRCWSAQPAERPNaDESLLKSL 264
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
510-773 6.46e-18

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: 84.30  E-value: 6.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYegLVIGlpgDSSPLQVAIKTLPELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14069   3 WDLVQTLGEGAFGEVF--LAVN---RNTEEAVAVKFVDMKRAPGDCPENIKkEVCIQKMLSHKNVVRFYGHRREGEFQYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMksFLRhSRPHLGQPSPLVMRDLLQLaqdIAqGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMa 668
Cdd:cd14069  78 FLEYASGGEL--FDK-IEPDVGMPEDVAQFYFQQL---MA-GLKYLHSCGITHRDIKPENLLLDEND---NLKISDFGL- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 rdiyrASYYRRGDRALLPVK------WMPPEAFLEGIF-TSKTDSWSFGVLLweiFSL--GYMPY--PGRTNQEVLDFVV 737
Cdd:cd14069 147 -----ATVFRYKGKERLLNKmcgtlpYVAPELLAKKKYrAEPVDVWSCGIVL---FAMlaGELPWdqPSDSCQEYSDWKE 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 738 GGG-RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASI 773
Cdd:cd14069 219 NKKtYLTPWKKIDTAALSLLRKILTENPNKRITIEDI 255
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
516-776 6.77e-18

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: 84.47  E-value: 6.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVY------EGLVIglpgdssplqvaIKTL---PELCSPQDELdfLMEALIISKFRHQNIVRCVGLSLRATPR 586
Cdd:cd14027   1 LDSGGFGKVSlcfhrtQGLVV------------LKTVytgPNCIEHNEAL--LEEGKMMNRLRHSRVVKLLGVILEEGKY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHSrphlgqPSPLVMRDLLQLaqDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFG 666
Cdd:cd14027  67 SLVMEYMEKGNLMHVLKKV------SVPLSVKGRIIL--EIIEGMAYLHGKGVIHKDLKPENILVD---NDFHIKIADLG 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASYYRRGDRALLPVK-----------WMPPEAF--LEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14027 136 LASFKMWSKLTKEEHNEQREVDgtakknagtlyYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFA-NKEPYENAINEDQI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 734 DFVVGGGRM----DPPRGCPGPVYRIMTQCWQHEPELRPSFASILER 776
Cdd:cd14027 215 IMCIKSGNRpdvdDITEYCPREIIDLMKLCWEANPEARPTFPGIEEK 261
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
516-777 1.00e-17

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: 83.85  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLpgdssplQVAIKTLPELCSpqdeLDFLMEALII-SKFRHQNIVRCVGLSLRatPRLILLELMS 594
Cdd:cd14068   2 LGDGGFGSVYRAVYRGE-------DVAVKIFNKHTS----FRLLRQELVVlSHLHHPSLVALLAAGTA--PRMLVMELAP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRPHLGQPsplvmrdlLQ--LAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSR--VAKIGDFGMA-- 668
Cdd:cd14068  69 KGSLDALLQQDNASLTRT--------LQhrIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCaiIAKIADYGIAqy 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 --RDIYRASYYRRGDRAllpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGY-----MPYPgrtnQEVLDFVVGGGR 741
Cdd:cd14068 141 ccRMGIKTSEGTPGFRA-------PEVARGNVIYNQQADVYSFGLLLYDILTCGErivegLKFP----NEFDELAIQGKL 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 742 MDPPR--GC-PGP-VYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14068 210 PDPVKeyGCaPWPgVEALIKDCLKENPQCRPTSAQVFDIL 249
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
516-770 1.04e-17

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: 83.91  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14202  10 IGHGAFAVVFKGR----HKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLrHSRPHLGQPSplvMRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAG-----PSRV-AKIGDFGMAR 669
Cdd:cd14202  86 GDLADYL-HTMRTLSEDT---IRLFLQ---QIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnPNNIrIKIADFGFAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 diYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDP--PRG 747
Cdd:cd14202 159 --YLQNNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSLSPniPRE 234
                       250       260
                ....*....|....*....|...
gi 42544153 748 CPGPVYRIMTQCWQHEPELRPSF 770
Cdd:cd14202 235 TSSHLRQLLLGLLQRNQKDRMDF 257
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
516-774 1.26e-17

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: 83.64  E-value: 1.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLV----------IGLpgDSSPLQVAIKTLPELcspQDELDfLMEALiiskfRHQNIVRCVGLSLRATP 585
Cdd:cd06631   9 LGKGAYGTVYCGLTstgqliavkqVEL--DTSDKEKAEKEYEKL---QEEVD-LLKTL-----KHVNIVGYLGTCLEDNV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMSGGDMKSFLRhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDF 665
Cdd:cd06631  78 VSIFMEFVPGGSIASILA-------RFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLM---PNGVIKLIDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRASYYRRGDRALLPVK----WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYpGRTNQEVLDFVVGGGR 741
Cdd:cd06631 148 GCAKRLCINLSSGSQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPW-ADMNPMAAIFAIGSGR 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 742 MDPPR---GCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd06631 226 KPVPRlpdKFSPEARDFVHACLTRDQDERPSAEQLL 261
Pkinase pfam00069
Protein kinase domain;
511-775 1.29e-17

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 82.68  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLP-ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKAKHR-----DTGKIVAIKKIKkEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   590 LELMSGGDMKSFLRHSRphlgqpsplvmrdllqlaqdiaqgchYLEENHFihRDIAArnCLLScagpsrvakigdfGMAR 669
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKG--------------------------AFSEREA--KFIMK--QILE-------------GLES 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   670 DIYRASYyrRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRM--DPPRG 747
Cdd:pfam00069 114 GSSLTTF--VGTPW-----YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELIIDQPYAfpELPSN 185
                         250       260
                  ....*....|....*....|....*...
gi 42544153   748 CPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:pfam00069 186 LSEEAKDLLKKLLKKDPSKRLTATQALQ 213
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
516-777 1.71e-17

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: 83.43  E-value: 1.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLP-------------GDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd14000   2 LGDGGFGSVYRASYKGEPvavkifnkhtssnFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 atPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLL-SCAGPSRV-A 660
Cdd:cd14000  82 --PLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQ---RIALQVADGLRYLHSAMIIYRDLKSHNVLVwTLYPNSAIiI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYYRRGDRAllpvKWMPPE-AFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVvgg 739
Cdd:cd14000 157 KIADYGISRQCCRMGAKGSEGTP----GFRAPEiARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIH--- 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42544153 740 GRMDPPRGCPGPVY-----RIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14000 230 GGLRPPLKQYECAPwpeveVLMKKCWKENPQQRPTAVTVVSIL 272
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
516-718 2.03e-17

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 83.31  E-value: 2.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglpgdSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14664   1 IGRGGAGTVYKGVM------PNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLrHSRPHLGQPSPLVMRDllQLAQDIAQGCHYLEEN---HFIHRDIAARNCLLScagPSRVAKIGDFGMARDI- 671
Cdd:cd14664  75 GSLGELL-HSRPESQPPLDWETRQ--RIALGSARGLAYLHHDcspLIIHRDVKSNNILLD---EEFEAHVADFGLAKLMd 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 672 YRASYYRRGDRAllPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd14664 149 DKDSHVMSSVAG--SYGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT 193
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
516-724 4.43e-17

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: 82.70  E-value: 4.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVyeglvIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIV--RCV--GLSLRATPRLILL- 590
Cdd:cd14038   2 LGTGGFGNV-----LRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVaaRDVpeGLQKLAPNDLPLLa 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 -ELMSGGDMKSFLRHSRPHLGqpsplvMRD--LLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScAGPSR-VAKIGDFG 666
Cdd:cd14038  77 mEYCQGGDLRKYLNQFENCCG------LREgaILTLLSDISSALRYLHENRIIHRDLKPENIVLQ-QGEQRlIHKIIDLG 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 667 MARDIYRASYYRRGDRALlpvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14038 150 YAKELDQGSLCTSFVGTL---QYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
517-775 5.83e-17

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: 81.58  E-value: 5.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 517 GHGAFGEVYegLVIGLpgDSSPLqVAIKTLP-ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd06626   9 GEGTFGKVY--TAVNL--DTGEL-MAMKEIRfQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRphlGQPSPLVMRDLLQLAQDIAqgchYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRAS 675
Cdd:cd06626  84 GTLEELLRHGR---ILDEAVIRVYTLQLLEGLA----YLHENGIVHRDIKPANIFLDSNG---LIKLGDFGSAVKLKNNT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRALLPV---KWMPPEAFLEGIFTSK---TDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGrMDPPrgCP 749
Cdd:cd06626 154 TTMAPGEVNSLVgtpAYMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPWSELDNEWAIMYHVGMG-HKPP--IP 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 750 GPV------YRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06626 230 DSLqlspegKDFLSRCLESDPKKRPTASELLD 261
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
516-775 9.17e-17

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: 81.10  E-value: 9.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLpELCSPQDELdFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd06614   8 IGEGASGEVYKATDRA-----TGKEVAIKKM-RLRKQNKEL-IINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQPS-PLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRA 674
Cdd:cd06614  81 GSLTDIITQNPVRMNESQiAYVCREVLQ-------GLEYLHSQNVIHRDIKSDNILLSKDG---SVKLADFGFAAQLTKE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 675 SYYRR---GDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGG--RMDPPRGCP 749
Cdd:cd06614 151 KSKRNsvvGTPY-----WMAPEVIKRKDYGPKVDIWSLGIMCIEMAE-GEPPYLEEPPLRALFLITTKGipPLKNPEKWS 224
                       250       260
                ....*....|....*....|....*.
gi 42544153 750 GPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06614 225 PEFKDFLNKCLVKDPEKRPSAEELLQ 250
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
511-775 1.00e-16

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: 81.25  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLpELCSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd06640   7 TKLERIGKGSFGEVFKGI-----DNRTQQVVAIKII-DLEEAEDEIeDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRhsrphlgqPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMAR 669
Cdd:cd06640  81 MEYLGGGSALDLLR--------AGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGD---VKLADFGVAG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVLDFVvgggRMDPPRGCP 749
Cdd:cd06640 150 QL-TDTQIKRNTFVGTPF-WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMHPMRVLFLI----PKNNPPTLV 222
                       250       260       270
                ....*....|....*....|....*....|
gi 42544153 750 GPVYR----IMTQCWQHEPELRPSFASILE 775
Cdd:cd06640 223 GDFSKpfkeFIDACLNKDPSFRPTAKELLK 252
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
510-777 1.07e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 80.72  E-value: 1.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGLP-GDSSPLQVAIKTLPELCSPQDElDFLMEALIISKFRHQNIVRCVGLSLrATPRLI 588
Cdd:cd14208   1 LTFMESLGKGSFTKIYRGLRTDEEdDERCETEVLLKVMDPTHGNCQE-SFLEAASIMSQISHKHLVLLHGVCV-GKDSIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSrphlGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS---CAGPSRVAKIGDF 665
Cdd:cd14208  79 VQEFVCHGALDLYLKKQ----QQKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSregDKGSPPFIKLSDP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYrasyyrrgDRALLP--VKWMPPEAFLEG-IFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRM 742
Cdd:cd14208 155 GVSIKVL--------DEELLAerIPWVAPECLSDPqNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQL 226
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 743 DPPRGCpgPVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd14208 227 PAPHWI--ELASLIQQCMSYNPLLRPSFRAIIRDL 259
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
564-775 1.27e-16

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: 80.66  E-value: 1.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 564 IISKFRHQNIVRCVG-LSLRATPRL-ILLELMSGGDMKSFLRHSRPHlGQ--PSPLVMRDLLQLAQDIaQGCHYLEENH- 638
Cdd:cd08217  52 ILRELKHPNIVRYYDrIVDRANTTLyIVMEYCEGGDLAQLIKKCKKE-NQyiPEEFIWKIFTQLLLAL-YECHNRSVGGg 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 639 -FIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRAS----------YYrrgdrallpvkwMPPEAFLEGIFTSKTDSW 707
Cdd:cd08217 130 kILHRDLKPANIFLDSDN---NVKLGDFGLARVLSHDSsfaktyvgtpYY------------MSPELLNEQSYDEKSDIW 194
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 708 SFGVLLWEIFSLGyMPYPGRtNQEVLDFVVGGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd08217 195 SLGCLIYELCALH-PPFQAA-NQLELAKKIKEGKFPRiPSRYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
516-724 1.42e-16

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: 80.96  E-value: 1.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVyeglVIGLPGDSSpLQVAIKTLPELCSPQDE--LDFLMEALIISKFRHQNIVRCV----GLSLRATPRLIL 589
Cdd:cd13989   1 LGSGGFGYV----TLWKHQDTG-EYVAIKKCRQELSPSDKnrERWCLEVQIMKKLNHPNVVSARdvppELEKLSPNDLPL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 L--ELMSGGDMKSFLrhSRPHlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGM 667
Cdd:cd13989  76 LamEYCSGGDLRKVL--NQPE--NCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGY 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 668 ARDIyrasyyrrgDRALL------PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd13989 152 AKEL---------DQGSLctsfvgTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
512-786 1.62e-16

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: 80.43  E-value: 1.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIgLPGDSsplqVAIKTLPelCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06613   4 LIQRIGSGTYGDVYKARNI-ATGEL----AAVKVIK--LEPGDDFEIIQqEISMLKECRHPNIVAYFGSYLRRDKLWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLqlaqdiaQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd06613  77 EYCGGGSLQDIYQVTGPLSELQIAYVCRETL-------KGLAYLHSTGKIHRDIKGANILLTEDGD---VKLADFGVSAQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IyRASYYRRGDRALLPVkWMPPEAFLE---GIFTSKTDSWSFGVLLWEI-------FSLgympYPGRtnqeVLdFVVGGG 740
Cdd:cd06613 147 L-TATIAKRKSFIGTPY-WMAPEVAAVerkGGYDGKCDIWALGITAIELaelqppmFDL----HPMR----AL-FLIPKS 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544153 741 RMDPP------RGCPGpVYRIMTQCWQHEPELRPSFASILerlqyctQDPDV 786
Cdd:cd06613 216 NFDPPklkdkeKWSPD-FHDFIKKCLTKNPKKRPTATKLL-------QHPFV 259
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
558-773 1.70e-16

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: 80.39  E-value: 1.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 558 FLMEALIISKFRHQNIVRCVGLsLRATPRL-ILLELMSGGDMKSFLRHSRPHLgqpsPLVMRdlLQLAQDIAQGCHYLEE 636
Cdd:cd14221  37 FLKEVKVMRCLEHPNVLKFIGV-LYKDKRLnFITEYIKGGTLRGIIKSMDSHY----PWSQR--VSFAKDIASGMAYLHS 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 637 NHFIHRDIAARNCLLSCAGPSRVAkigDFGMARDIYRASYYRRGDRALLPVK------------WMPPEAFLEGIFTSKT 704
Cdd:cd14221 110 MNIIHRDLNSHNCLVRENKSVVVA---DFGLARLMVDEKTQPEGLRSLKKPDrkkrytvvgnpyWMAPEMINGRSYDEKV 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 705 DSWSFGVLLWEIFSL-----GYMPypgRTNQEVLDFVVGGGRMDPPrGCPGPVYRIMTQCWQHEPELRPSFASI 773
Cdd:cd14221 187 DVFSFGIVLCEIIGRvnadpDYLP---RTMDFGLNVRGFLDRYCPP-NCPPSFFPIAVLCCDLDPEKRPSFSKL 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
514-775 2.11e-16

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: 80.51  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPE----LCSPQ---DELDFLMEALIISKFRHQNIVRCVGLSLRATPR 586
Cdd:cd14084  12 RTLGSGACGEVKLAY-----DKSTCKKVAIKIINKrkftIGSRReinKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHSRpHLGQP-SPLVMRDLLQLAQdiaqgchYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDF 665
Cdd:cd14084  87 YIVLELMEGGELFDRVVSNK-RLKEAiCKLYFYQMLLAVK-------YLHSNGIIHRDLKPENVLLSSQEEECLIKITDF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIyrasyyrrGDRALL-----PVKWMPPEAFLEGI---FTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd14084 159 GLSKIL--------GETSLMktlcgTPTYLAPEVLRSFGtegYTRAVDCWSLGVILFICLS-GYPPFSEEYTQMSLKEQI 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42544153 738 GGGRmdpprgcpgpvYRIMTQCWQH---------------EPELRPSFASILE 775
Cdd:cd14084 230 LSGK-----------YTFIPKAWKNvseeakdlvkkmlvvDPSRRPSIEEALE 271
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
516-775 2.17e-16

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: 80.14  E-value: 2.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglPGDSSPLqVAIKTLPELCSPQDELDFL----MEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd06632   8 LGSGSFGSVYEGF----NGDTGDF-FAVKEVSLVDDDKKSRESVkqleQEIALLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHlgqPSPLVMrdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDI 671
Cdd:cd06632  83 YVPGGSIHKLLQRYGAF---EEPVIR----LYTRQILSGLAYLHSRNTVHRDIKGANILVDTNG---VVKLADFGMAKHV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYyrrgdraLLPVK----WMPPEAFLE--GIFTSKTDSWSFG--VL-----------------LWEIFSLGYMP-YP 725
Cdd:cd06632 153 EAFSF-------AKSFKgspyWMAPEVIMQknSGYGLAVDIWSLGctVLematgkppwsqyegvaaIFKIGNSGELPpIP 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 726 GRTNQEVLDFVvgggrmdpprgcpgpvyrimTQCWQHEPELRPSFASILE 775
Cdd:cd06632 226 DHLSPDAKDFI--------------------RLCLQRDPEDRPTASQLLE 255
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
516-724 2.32e-16

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: 80.35  E-value: 2.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEglvigLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRC------VGLSLRATPrLIL 589
Cdd:cd14039   1 LGTGGFGNVCL-----YQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKAcdvpeeMNFLVNDVP-LLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRPHLGqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMAR 669
Cdd:cd14039  75 MEYCSGGDLRKLLNKPENCCG----LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAK 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 670 DIYRASYYRRGDRALlpvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14039 151 DLDQGSLCTSFVGTL---QYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPF 201
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
512-769 3.59e-16

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: 79.23  E-value: 3.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPelcSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd06612   7 ILEKLGEGSYGSVYKAIHK-----ETGQVVAIKVVP---VEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDI 671
Cdd:cd06612  79 YCGAGSVSDIMKITN------KTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEG---QAKLADFGVSGQL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 yrasYYRRGDRALL---PVkWMPPEAFLEGIFTSKTDSWSFGVLLWE----------------IFSLGYMPYPGRTN--- 729
Cdd:cd06612 150 ----TDTMAKRNTVigtPF-WMAPEVIQEIGYNNKADIWSLGITAIEmaegkppysdihpmraIFMIPNKPPPTLSDpek 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 730 --QEVLDFVvgggrmdpprgcpgpvyrimTQCWQHEPELRPS 769
Cdd:cd06612 225 wsPEFNDFV--------------------KKCLVKDPEERPS 246
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
513-734 5.59e-16

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: 79.53  E-value: 5.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIGlPGDssplQVAIKTLPElcspQDELD-----FLMEALIISKFRHQNIVRCVGL-----SLR 582
Cdd:cd07840   4 IAQIGEGTYGQVYKARNKK-TGE----LVALKKIRM----ENEKEgfpitAIREIKLLQKLDHPNVVRLKEIvtskgSAK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLIL-LELMSGgDMKSFLRHSRPHLGQPS-PLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGpsrVA 660
Cdd:cd07840  75 YKGSIYMvFEYMDH-DLTGLLDNPEVKFTESQiKCYMKQLLE-------GLQYLHSNGILHRDIKGSNILINNDG---VL 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 661 KIGDFGMARdiyraSYYRRGDRALLPV---KWM-PPEAFL-EGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLD 734
Cdd:cd07840 144 KLADFGLAR-----PYTKENNADYTNRvitLWYrPPELLLgATRYGPEVDMWSVGCILAELF-TGKPIFQGKTELEQLE 216
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
512-776 6.23e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 78.48  E-value: 6.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVyeglvIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVrCVGLSLRATPRL-ILL 590
Cdd:cd08219   4 VLRVVGEGSFGRA-----LLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIV-AFKESFEADGHLyIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGqPSPLVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd08219  78 EYCDGGDLMQKIKLQRGKLF-PEDTILQWFVQ----MCLGVQHIHEKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRASYYrrgdrALLPVK---WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYmPYPGRTNQEVLDFVVGGGRMDPPRG 747
Cdd:cd08219 150 LTSPGAY-----ACTYVGtpyYVPPEIWENMPYNNKSDIWSLGCILYELCTLKH-PFQANSWKNLILKVCQGSYKPLPSH 223
                       250       260
                ....*....|....*....|....*....
gi 42544153 748 CPGPVYRIMTQCWQHEPELRPSFASILER 776
Cdd:cd08219 224 YSYELRSLIKQMFKRNPRSRPSATTILSR 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
513-775 1.24e-15

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: 77.77  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYegLVIGLPgdsSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd06605   6 LGELGEGNGGVVS--KVRHRP---SGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHsrphlGQPSPLvmRDLLQLAQDIAQGCHYLEENH-FIHRDIAARNCLLSCAGPsrvAKIGDFG----- 666
Cdd:cd06605  81 MDGGSLDKILKE-----VGRIPE--RILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQ---VKLCDFGvsgql 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 ---MARDIYRASYYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQ------EVLDFVV 737
Cdd:cd06605 151 vdsLAKTFVGTRSY------------MAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFPYPPPNAKpsmmifELLSYIV 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 738 gggRMDPPR----GCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06605 218 ---DEPPPLlpsgKFSPDFQDFVSQCLQKDPTERPSYKELME 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
513-731 1.51e-15

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: 77.72  E-value: 1.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYeglviglpgdssplQV---------AIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd13996  11 IELLGSGGFGSVY--------------KVrnkvdgvtyAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLrHSRPHlgqpSPLVMRDL-LQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVAKI 662
Cdd:cd13996  77 PPLYIQMELCEGGTLRDWI-DRRNS----SSKNDRKLaLELFKQILKGVSYIHSKGIVHRDLKPSNIFLD--NDDLQVKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLP------------VKWMPPEAFLEGIFTSKTDSWSFGVLLWEifslgyMPYPGRTNQ 730
Cdd:cd13996 150 GDFGLATSIGNQKRELNNLNNNNNgntsnnsvgigtPLYASPEQLDGENYNEKADIYSLGIILFE------MLHPFKTAM 223

                .
gi 42544153 731 E 731
Cdd:cd13996 224 E 224
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
512-746 1.76e-15

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: 77.30  E-value: 1.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLviglpgDSSPLQVAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd14161   7 FLETLGKGTYGRVKKAR------DSSGRLVAIKSIrkDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMAr 669
Cdd:cd14161  81 MEYASRGDLYDYISERQR-------LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN---IKIADFGLS- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRasyyrrGDRALLPVKWMP----PEAFLEGIFTS-KTDSWSFGVLLWeIFSLGYMPYPGRTNQEVLDFVVGGGRMDP 744
Cdd:cd14161 150 NLYN------QDKFLQTYCGSPlyasPEIVNGRPYIGpEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGAYREP 222

                ..
gi 42544153 745 PR 746
Cdd:cd14161 223 TK 224
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
541-773 4.65e-15

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: 76.27  E-value: 4.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 541 VAIK--TLPELCSPQ--DELDFLMEAliiskfRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSrphlGQPSPLV 616
Cdd:cd13992  28 VAIKhiTFSRTEKRTilQELNQLKEL------VHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNR----EIKMDWM 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 617 MRdlLQLAQDIAQGCHYLEeNHFI--HRDIAARNCLLScagpSR-VAKIGDFGMARdIYRASYYRRGDRALLPVK--WMP 691
Cdd:cd13992  98 FK--SSFIKDIVKGMNYLH-SSSIgyHGRLKSSNCLVD----SRwVVKLTDFGLRN-LLEEQTNHQLDEDAQHKKllWTA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 692 PEaFLEGIFTS-----KTDSWSFGVLLWEIfsLGYM-PYPGRTNQEVLDFVVGGGrMDPPR------GCPGP--VYRIMT 757
Cdd:cd13992 170 PE-LLRGSLLEvrgtqKGDVYSFAIILYEI--LFRSdPFALEREVAIVEKVISGG-NKPFRpelavlLDEFPprLVLLVK 245
                       250
                ....*....|....*.
gi 42544153 758 QCWQHEPELRPSFASI 773
Cdd:cd13992 246 QCWAENPEKRPSFKQI 261
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
512-774 6.21e-15

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: 75.53  E-value: 6.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVY------EGLVIGLPgdssplQVAIKTLpelcSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATP 585
Cdd:cd08529   4 ILNKLGKGSFGVVYkvvrkvDGRVYALK------QIDISRM----SRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMSGGDMKSFLRHSRphlGQPSP--LVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIG 663
Cdd:cd08529  74 LNIVMEYAENGDLHSLIKSQR---GRPLPedQIWKFFIQ----TLLGLSHLHSKKILHRDIKSMNIFLDKGDN---VKIG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFG----------MARDIYRASYYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYmPYPGRtNQEVL 733
Cdd:cd08529 144 DLGvakilsdttnFAQTIVGTPYY------------LSPELCEDKPYNEKSDVWALGCVLYELCTGKH-PFEAQ-NQGAL 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 734 DFVVGGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd08529 210 ILKIVRGKYPPiSASYSQDLSQLIDSCLTKDYRQRPDTTELL 251
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
513-774 6.51e-15

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: 75.50  E-value: 6.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVY--EGLVIGLpgdsspLQVAIKTLPELCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRATPRLIL 589
Cdd:cd13997   5 LEQIGSGSFSEVFkvRSKVDGC------LYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMAR 669
Cdd:cd13997  79 MELCENGSLQDALEE----LSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG---TCKIGDFGLAT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRASYYRRGDRallpvKWMPPEaFLEGIFT--SKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVldfvvgggRMDPPRG 747
Cdd:cd13997 152 RLETSGDVEEGDS-----RYLAPE-LLNENYThlPKADIFSLGVTVYEAATGEPLPRNGQQWQQL--------RQGKLPL 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 748 CPGPVY-----RIMTQCWQHEPELRPSFASIL 774
Cdd:cd13997 218 PPGLVLsqeltRLLKVMLDPDPTRRPTADQLL 249
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
514-775 7.28e-15

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: 75.38  E-value: 7.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGlviglPGDSSPLQVAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd14116  11 RPLGKGKFGNVYLA-----REKQSKFILALKVLfkAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHLGQPSPLVMRDLlqlaqdiAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMArdi 671
Cdd:cd14116  86 YAPLGTVYRELQKLSKFDEQRTATYITEL-------ANALSYCHSKRVIHRDIKPENLLLGSAGE---LKIADFGWS--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYYRRGDRALlPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPYPGRTNQEVL-----------DFVVGGG 740
Cdd:cd14116 153 VHAPSSRRTTLCG-TLDYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETYkrisrveftfpDFVTEGA 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42544153 741 RmdpprgcpgpvyRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14116 231 R------------DLISRLLKHNPSQRPMLREVLE 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
511-775 1.07e-14

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: 74.96  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELdFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06647  10 TRFEKIGQGASGTVYTAIDV-----ATGQEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGQPSPlVMRDLLQLAQdiaqgchYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd06647  84 EYLAGGSLTDVVTETCMDEGQIAA-VCRECLQALE-------FLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFCAQ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMD-PPRGCP 749
Cdd:cd06647 153 I-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTPElQNPEKL 229
                       250       260
                ....*....|....*....|....*..
gi 42544153 750 GPVYR-IMTQCWQHEPELRPSFASILE 775
Cdd:cd06647 230 SAIFRdFLNRCLEMDVEKRGSAKELLQ 256
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
511-724 1.21e-14

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: 74.91  E-value: 1.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELCSPQDELD-FL-MEALIISKFRHQNIVRCVGLsLRATPRL- 587
Cdd:cd14080   3 RLGKTIGEGSYSKVKLAEYTK---SGLKEKVACKIIDKKKAPKDFLEkFLpRELEILRKLRHPNIIQVYSI-FERGSKVf 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLlqlaqdiAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGM 667
Cdd:cd14080  79 IFMEYAEHGDLLEYIQKRGALSESQARIWFRQL-------ALAVQYLHSLDIAHRDLKCENILLD---SNNNVKLSDFGF 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 668 ARdiyrasYYRRGDRALL------PVKWMPPEaFLEGI--FTSKTDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14080 149 AR------LCPDDDGDVLsktfcgSAAYAAPE-ILQGIpyDPKKYDIWSLGVILY-IMLCGSMPF 205
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
513-716 1.62e-14

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 75.44  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDE--LDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06634  20 LREIGHGSFGAVYFARDV-----RNNEVVAIKKMSYSGKQSNEkwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARD 670
Cdd:cd06634  95 EYCLGSASDLLEVHKKP-------LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPG---LVKLGDFGSASI 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42544153 671 IYRASYYrrgdraLLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEI 716
Cdd:cd06634 165 MAPANSF------VGTPYWMAPEVILamdEGQYDGKVDVWSLGITCIEL 207
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
510-774 1.64e-14

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 74.59  E-value: 1.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGLPGDSSPL---QVAIKTLPELCSPQDE---LDFLMEALIISKFRHQNIVRCVGLSLRA 583
Cdd:cd05077   1 IVQGEHLGRGTRTQIYAGILNYKDDDEDEGysyEKEIKVILKVLDPSHRdisLAFFETASMMRQVSHKHIVLLYGVCVRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMSGGDMKSFLRHsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL------SCAGPs 657
Cdd:cd05077  81 VENIMVEEFVEFGPLDLFMHR------KSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLaregidGECGP- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 rVAKIGDFGMArdIYRASYYRRGDRallpVKWMPPEAFLEG-IFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFV 736
Cdd:cd05077 154 -FIKLSDPGIP--ITVLSRQECVER----IPWIAPECVEDSkNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFY 226
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 737 VGGGRMDPPrGCPgPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd05077 227 EGQCMLVTP-SCK-ELADLMTHCMNYDPNQRPFFRAIM 262
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
516-716 1.72e-14

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: 74.68  E-value: 1.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGlviglPGDSSPLQVAIKTLPElcSPQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd06643  13 LGDGAFGKVYKA-----QNKETGILAAAKVIDT--KSEEELeDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKS-FLRHSRPhLGQPSPLVmrdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDIYR 673
Cdd:cd06643  86 GGAVDAvMLELERP-LTEPQIRV------VCKQTLEALVYLHENKIIHRDLKAGNILFTLDGD---IKLADFGVSAKNTR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42544153 674 AsyYRRGDRALLPVKWMPPEAFL-----EGIFTSKTDSWSFGVLLWEI 716
Cdd:cd06643 156 T--LQRRDSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEM 201
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
507-718 1.92e-14

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: 74.31  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANVTLLRALGHGAFGEVYeglvIGLPGDSSPlQVAIKTL---PELCSPQDELDFL-MEALIISKFRHQNIVRCVGLsLR 582
Cdd:cd06652   1 PTNWRLGKLLGQGAFGRVY----LCYDADTGR-ELAVKQVqfdPESPETSKEVNALeCEIQLLKNLLHERIVQYYGC-LR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRL---ILLELMSGGDMKSFLRHsrphLGQPSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrv 659
Cdd:cd06652  75 DPQERtlsIFMEYMPGGSIKDQLKS----YGALTENVTR---KYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGN--- 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFGMARDIYRASYYRRGDRALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd06652 145 VKLGDFGASKRLQTICLSGTGMKSVTGTPyWMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
516-775 2.05e-14

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: 74.39  E-value: 2.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYeglvigLPGDSSPLQVAIKTLPELCSpQDEL-DFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd06611  13 LGDGAFGKVY------KAQHKETGLFAAAKIIQIES-EEELeDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRPHLGQPS-PLVMRDLLqlaqdiaQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAkigDFGMA----- 668
Cdd:cd06611  86 GGALDSIMLELERGLTEPQiRYVCRQML-------EALNFLHSHKVIHRDLKAGNILLTLDGDVKLA---DFGVSaknks 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 ----RDIYRASYYrrgdrallpvkWMPP-----EAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd06611 156 tlqkRDTFIGTPY-----------WMAPevvacETFKDNPYDYKADIWSLGITLIEL-AQMEPPHHELNPMRVLLKILKS 223
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42544153 740 G--RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06611 224 EppTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLK 261
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
516-775 2.93e-14

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: 73.96  E-value: 2.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlPGDssPLQVAIKTLPELCSPQ-DELDFLMEALI---ISKFR---HQNIVRCVGLSLRATPRLI 588
Cdd:cd06629   9 IGKGTYGRVYLAMNAT-TGE--MLAVKQVELPKTSSDRaDSRQKTVVDALkseIDTLKdldHPNIVQYLGFEETEDYFSI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHsrphLGQPSPLVMRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:cd06629  86 FLEYVPGGSIGSCLRK----YGKFEEDLVRFFTR---QILDGLAYLHSKGILHRDLKADNILVDLEG---ICKISDFGIS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 R---DIYRASyyrrGDRALL-PVKWMPPEAF--LEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLdFVVGGGRM 742
Cdd:cd06629 156 KksdDIYGNN----GATSMQgSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAM-FKLGNKRS 229
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42544153 743 DPPrgCPGPV------YRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06629 230 APP--VPEDVnlspeaLDFLNACFAIDPRDRPTAAELLS 266
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
516-735 2.98e-14

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: 73.89  E-value: 2.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14201  14 VGHGAFAVVFKGR----HRKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSrphlGQPSPLVMRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVA------KIGDFGMAR 669
Cdd:cd14201  90 GDLADYLQAK----GTLSEDTIRVFLQ---QIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSvsgiriKIADFGFAR 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 670 diYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDF 735
Cdd:cd14201 163 --YLQSNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDLRMF 224
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
509-769 3.52e-14

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: 74.00  E-value: 3.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEglvIGLPGdsSPLQVAIKTLpeLCSPQDEL--DFLMEALIISKFRHQNIVRCVGLSL-RATP 585
Cdd:cd06621   2 KIVELSSLGEGAGGSVTK---CRLRN--TKTIFALKTI--TTDPNPDVqkQILRELEINKSCASPYIVKYYGAFLdEQDS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RL-ILLELMSGGDMKSFLRHSRPHLGQPSPLVmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGD 664
Cdd:cd06621  75 SIgIAMEYCEGGSLDSIYKKVKKKGGRIGEKV---LGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ---VKLCD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FG--------MARDIYRASYYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQ-----E 731
Cdd:cd06621 149 FGvsgelvnsLAGTFTGTSYY------------MAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPPEGEPplgpiE 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 732 VLDFVVgggRMDPP--RGCPG-------PVYRIMTQCWQHEPELRPS 769
Cdd:cd06621 216 LLSYIV---NMPNPelKDEPEngikwseSFKDFIEKCLEKDGTRRPG 259
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
516-778 3.86e-14

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 73.93  E-value: 3.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPgdssplqVAIKTLPelcsPQDELDFLMEALIISKF--RHQNIVRCVGLSLRATPR-----LI 588
Cdd:cd14054   3 IGQGRYGTVWKGSLDERP-------VAVKVFP----ARHRQNFQNEKDIYELPlmEHSNILRFIGADERPTADgrmeyLL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSrphlgqpsPLVMRDLLQLAQDIAQGCHYLEEN---------HFIHRDIAARNCL----LSCAg 655
Cdd:cd14054  72 VLEYAPKGSLCSYLREN--------TLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLvkadGSCV- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 656 psrvakIGDFGMARDIYRASYYRR----GDRALL----PVKWMPPEaFLEGI--------FTSKTDSWSFGVLLWEIFSL 719
Cdd:cd14054 143 ------ICDFGLAMVLRGSSLVRGrpgaAENASIsevgTLRYMAPE-VLEGAvnlrdcesALKQVDVYALGLVLWEIAMR 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 720 GYMPYPGRT--------NQEV--------LDFVVGGGRMDP------PRGCPGP--VYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14054 216 CSDLYPGESvppyqmpyEAELgnhptfedMQLLVSREKARPkfpdawKENSLAVrsLKETIEDCWDQDAEARLTALCVEE 295

                ...
gi 42544153 776 RLQ 778
Cdd:cd14054 296 RLA 298
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
516-770 4.26e-14

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: 73.09  E-value: 4.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQ-VAIKtlpelCSPQDEL------DFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14121   3 LGSGTYATVYKAYRK-----SGAREvVAVK-----CVSKSSLnkasteNLLTEIELLKKLKHPHIVELKDFQWDEEHIYL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLrHSRPHLgqPSPLVMRDLLQLAQDIaqgcHYLEENHFIHRDIAARNCLLScAGPSRVAKIGDFGMA 668
Cdd:cd14121  73 IMEYCSGGDLSRFI-RSRRTL--PESTVRRFLQQLASAL----QFLREHNISHMDLKPQNLLLS-SRYNPVLKLADFGFA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RdiyrasYYRRGDRALL----PVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVvgggRMDP 744
Cdd:cd14121 145 Q------HLKPNDEAHSlrgsPL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKI----RSSK 212
                       250       260       270
                ....*....|....*....|....*....|...
gi 42544153 745 PRGCPgPVYRIMTQC-------WQHEPELRPSF 770
Cdd:cd14121 213 PIEIP-TRPELSADCrdlllrlLQRDPDRRISF 244
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
507-718 4.47e-14

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: 73.14  E-value: 4.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANVTLLRALGHGAFGEVYeglvIGLPGDSSPlQVAIKTLPELCSPQD---ELDFL-MEALIISKFRHQNIVRCVGLSLR 582
Cdd:cd06653   1 PVNWRLGKLLGRGAFGEVY----LCYDADTGR-ELAVKQVPFDPDSQEtskEVNALeCEIQLLKNLRHDRIVQYYGCLRD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPR--LILLELMSGGDMKSFLRhsrpHLGQPSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvA 660
Cdd:cd06653  76 PEEKklSIFVEYMPGGSVKDQLK----AYGALTENVTR---RYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGN---V 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 661 KIGDFGMARDIYRASYYRRGDRALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd06653 146 KLGDFGASKRIQTICMSGTGIKSVTGTPyWMSPEVISGEGYGRKADVWSVACTVVEMLT 204
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
511-729 5.03e-14

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: 72.65  E-value: 5.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLviglpgDSSPLQ-VAIKTL----PELCSPQDELDFLMEalIISKFRHQNIVRCVGL--SLRA 583
Cdd:cd05118   2 EVLRKIGEGAFGTVWLAR------DKVTGEkVAIKKIkndfRHPKAALREIKLLKH--LNDVEGHPNIVKLLDVfeHRGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRLILLELMsGGDMKSFLRHSRPHLgqPSPLVMRDLLQLAQDIAqgchYLEENHFIHRDIAARNCLLScaGPSRVAKIG 663
Cdd:cd05118  74 NHLCLVFELM-GMNLYELIKDYPRGL--PLDLIKSYLYQLLQALD----FLHSNGIIHRDLKPENILIN--LELGQLKLA 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 664 DFGMARDIYRASYYRRgdraLLPVKWMPPEAFLEGIF-TSKTDSWSFGVLLWEIFSlGYMPYPGRTN 729
Cdd:cd05118 145 DFGLARSFTSPPYTPY----VATRWYRAPEVLLGAKPyGSSIDIWSLGCILAELLT-GRPLFPGDSE 206
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
512-745 7.10e-14

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: 72.51  E-value: 7.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpgDSSPLQvAIKTLPE---LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14098   4 IIDRLGSGTFAEVKKAVEV----ETGKMR-AIKQIVKrkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRhsrPHLGQPSplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsRVAKIGDFGMA 668
Cdd:cd14098  79 VMEYVEGGDLMDFIM---AWGAIPE----QHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDP-VIVKISDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYRR--GDRALL-PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDPP 745
Cdd:cd14098 151 KVIHTGTFLVTfcGTMAYLaPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKRIRKGRYTQPP 229
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
516-778 7.66e-14

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: 72.73  E-value: 7.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGlpgdssplQVAIKTLPELCSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd14153   8 IGKGRFGQVYHGRWHG--------EVAIRLIDIERDNEEQLKaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAkIGDFGM--ARDIY 672
Cdd:cd14153  80 GRTLYSVVRDAK------VVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD---NGKVV-ITDFGLftISGVL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASyyRRGDRALLPVKWM-----------PPEAFLEGI-FTSKTDSWSFGVLLWEIFSlgyMPYPGRTN-QEVLDFVVGG 739
Cdd:cd14153 150 QAG--RREDKLRIQSGWLchlapeiirqlSPETEEDKLpFSKHSDVFAFGTIWYELHA---REWPFKTQpAEAIIWQVGS 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 740 GrMDP---PRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14153 225 G-MKPnlsQIGMGKEISDILLFCWAYEQEERPTFSKLMEMLE 265
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
504-775 8.52e-14

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: 72.76  E-value: 8.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANV-TLLRALGHGAFGEVYEGlviglPGDSSPLQVAIKTLPElcSPQDEL-DFLMEALIISKFRHQNIVRCVGLSL 581
Cdd:cd06644   7 DLDPNEVwEIIGELGDGAFGKVYKA-----KNKETGALAAAKVIET--KSEEELeDYMVEIEILATCNHPYIVKLLGAFY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 582 RATPRLILLELMSGGDMKSFLRHSRPHLGQPS-PLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPSRVA 660
Cdd:cd06644  80 WDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQiQVICRQMLE-------ALQYLHSMKIIHRDLKAGNVLLTLDGDIKLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 kigDFGMARDIYRAsyYRRGDRALLPVKWMPPEAFL-----EGIFTSKTDSWSFGVLLWEIFSLgympYPGRTNQEVLDF 735
Cdd:cd06644 153 ---DFGVSAKNVKT--LQRRDSFIGTPYWMAPEVVMcetmkDTPYDYKADIWSLGITLIEMAQI----EPPHHELNPMRV 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 736 VVGGGRMDPPR-GCP---GPVYR-IMTQCWQHEPELRPSFASILE 775
Cdd:cd06644 224 LLKIAKSEPPTlSQPskwSMEFRdFLKTALDKHPETRPSAAQLLE 268
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
510-786 9.04e-14

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: 72.57  E-value: 9.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLviglpgdSSPLQVaIKTLPELCSPQDELDF---LMEALIISKFRHQNIVRCVGLSLRATPR 586
Cdd:cd06622   3 IEVLDELGKGNYGSVYKVL-------HRPTGV-TMAMKEIRLELDESKFnqiIMELDILHKAVSPYIVDFYGAFFIEGAV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHSRPHLGQPSPLVMRdllqLAQDIAQGCHYLEENH-FIHRDIAARNCLLSCAGPsrvAKIGDF 665
Cdd:cd06622  75 YMCMEYMDAGSLDKLYAGGVATEGIPEDVLRR----ITYAVVKGLKFLKEEHnIIHRDVKPTNVLVNGNGQ---VKLCDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRA-SYYRRGDRAllpvkWMPPE------AFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEV---LDF 735
Cdd:cd06622 148 GVSGNLVASlAKTNIGCQS-----YMAPEriksggPNQNPTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIfaqLSA 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 736 VVGGgrmDPPR---GCPGPVYRIMTQCWQHEPELRPSFASILER---LQYCTQDPDV 786
Cdd:cd06622 222 IVDG---DPPTlpsGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHpwlVKYKNADVDM 275
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
513-711 9.19e-14

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: 72.10  E-value: 9.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYeglvigLPGDSSPLQ-VAIKTLPELCSPQDE--LDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd06607   6 LREIGHGSFGAVY------YARNKRTSEvVAIKKMSYSGKQSTEkwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LE--LMSGGDMKSFLRhsrphlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGM 667
Cdd:cd06607  80 MEycLGSASDIVEVHK---------KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPG---TVKLADFGS 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 668 ARDIYRASYYrrgdrALLPVkWMPPEAFL---EGIFTSKTDSWSFGV 711
Cdd:cd06607 148 ASLVCPANSF-----VGTPY-WMAPEVILamdEGQYDGKVDVWSLGI 188
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
511-793 1.01e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 72.83  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELdFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06654  23 TRFEKIGQGASGTVYTAMDV-----ATGQEVAIRQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVM 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGQPSPlVMRDLLQLAQdiaqgchYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd06654  97 EYLAGGSLTDVVTETCMDEGQIAA-VCRECLQALE-------FLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFCAQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGG--RMDPPRGC 748
Cdd:cd06654 166 I-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGtpELQNPEKL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILERLQYCTQDPdvLNSLLPM 793
Cdd:cd06654 243 SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKP--LSSLTPL 285
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
511-796 1.07e-13

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: 72.83  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGLPGdssplQVAIKTLPELCSPQDELdFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06655  22 TRYEKIGQGASGTVFTAIDVATGQ-----EVAIKQINLQKQPKKEL-IINEILVMKELKNPNIVNFLDSFLVGDELFVVM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGQPSPlVMRDLLQLAQdiaqgchYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd06655  96 EYLAGGSLTDVVTETCMDEAQIAA-VCRECLQALE-------FLHANQVIHRDIKSDNVLLGMDGS---VKLTDFGFCAQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGrmDPPRGCP- 749
Cdd:cd06655 165 I-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNG--TPELQNPe 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 750 --GPVYR-IMTQCWQHEPELRPSFASILERLQYCTQDPdvLNSLLPMELG 796
Cdd:cd06655 240 klSPIFRdFLNRCLEMDVEKRGSAKELLQHPFLKLAKP--LSSLTPLILA 287
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
511-793 1.13e-13

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 72.83  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELdFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06656  22 TRFEKIGQGASGTVYTAIDI-----ATGQEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGQpsplvmrdLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd06656  96 EYLAGGSLTDVVTETCMDEGQ--------IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFCAQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IyRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGG--RMDPPRGC 748
Cdd:cd06656 165 I-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGtpELQNPERL 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILERLQYCTQDPdvLNSLLPM 793
Cdd:cd06656 242 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKP--LSSLTPL 284
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
508-775 1.19e-13

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: 71.98  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 508 ANVTLLRALGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL 587
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATCLL---DRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRPHLGQ-PSPLVMRDLLQLaqdiaqgCHYLEENH---FIHRDIAARNCLLSCAGpsrVAKIG 663
Cdd:cd08228  79 IVLELADAGDLSQMIKYFKKQKRLiPERTVWKYFVQL-------CSAVEHMHsrrVMHRDIKPANVFITATG---VVKLG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARdiYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQ-------EVLDFv 736
Cdd:cd08228 149 DLGLGR--FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLfslcqkiEQCDY- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42544153 737 vgggrmdPPrgCPGPVY-----RIMTQCWQHEPELRPSFASILE 775
Cdd:cd08228 226 -------PP--LPTEHYseklrELVSMCIYPDPDQRPDIGYVHQ 260
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
513-778 1.40e-13

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: 72.26  E-value: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGlviglPGDSSPLQVAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd14026   2 LRYLSRGAFGTVSRA-----RHADWRVTVAIKCLklDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHLGQPSPLVMRDLlqlaQDIAQGCHYLEENH--FIHRDIAARNCLLScaGPSRVaKIGDFGMA 668
Cdd:cd14026  77 EYMTNGSLNELLHEKDIYPDVAWPLRLRIL----YEIALGVNYLHNMSppLLHHDLKTQNILLD--GEFHV-KIADFGLS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYRRGDRALL---PVKWMPPEAFLEGIFTS---KTDSWSFGVLLWEIFSLGYmPYPGRTNQ-EVLDFVVGGGR 741
Cdd:cd14026 150 KWRQLSISQSRSSKSAPeggTIIYMPPEEYEPSQKRRasvKHDIYSYAIIMWEVLSRKI-PFEEVTNPlQIMYSVSQGHR 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 742 MD----------PPRGCpgpVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14026 229 PDtgedslpvdiPHRAT---LINLIESGWAQNPDERPSFLKCLIELE 272
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
516-774 1.86e-13

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: 71.31  E-value: 1.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLMEAL-----IISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06630   8 LGTGAFSSCYQARDV-----KTGTLMAVKQVSFCRNSSSEQEEVVEAIreeirMMARLNHPNIVRMLGATQHKSHFNIFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHlgqPSPLVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsRVAKIGDFG---- 666
Cdd:cd06630  83 EWMAGGSVASLLSKYGAF---SENVIINYTLQ----ILRGLAYLHDNQIIHRDLKGANLLVDSTG--QRLRIADFGaaar 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASYYRrgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGR--TNQEVLDFVVGGGRMDP 744
Cdd:cd06630 154 LASKGTGAGEFQ--GQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPWNAEkiSNHLALIFKIASATTPP 230
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 745 --PRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd06630 231 piPEHLSPGLRDVTLRCLELQPEDRPPARELL 262
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
511-769 2.83e-13

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: 70.66  E-value: 2.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGlviglPGDSSPLQVAIKTLPELCSPQDELD-FLMEAL-IISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14164   3 TLGTTIGEGSFSKVKLA-----TSQKYCCKVAIKIVDRRRASPDFVQkFLPRELsILRRVNHPNIVQMFECIEVANGRLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHsrphLGQPSPLVMRDLLqlAQdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsRVAKIGDFGMA 668
Cdd:cd14164  78 IVMEAAATDLLQKIQE----VHHIPKDLARDMF--AQ-MVGAVNYLHDMNIVHRDLKCENILLSADD--RKIKIADFGFA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIY---RASYYRRGDRAllpvkWMPPEAFLEGIFTSKT-DSWSFGVLLWEIFSlGYMPYPG------RTNQEVLDFVVG 738
Cdd:cd14164 149 RFVEdypELSTTFCGSRA-----YTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFDEtnvrrlRLQQRGVLYPSG 222
                       250       260       270
                ....*....|....*....|....*....|.
gi 42544153 739 GGRMDPPRGcpgpvyrIMTQCWQHEPELRPS 769
Cdd:cd14164 223 VALEEPCRA-------LIRTLLQFNPSTRPS 246
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
514-773 3.59e-13

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: 70.60  E-value: 3.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPEL-CSPQDELDFLMEALIISKFRHQNIVRCVGLSlrATPRLILLEL 592
Cdd:cd14025   2 EKVGSGGFGQVYKVRHK-----HWKTWLAIKCPPSLhVDDSERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRhsrphlGQPSPLVMRdlLQLAQDIAQGCHYLE--ENHFIHRDIAARNCLLScaGPSRVaKIGDFGMAR- 669
Cdd:cd14025  75 METGSLEKLLA------SEPLPWELR--FRIIHETAVGMNFLHcmKPPLLHLDLKPANILLD--AHYHV-KISDFGLAKw 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 --DIYRASYYRRGDRALLpvKWMPPEAFLEG--IFTSKTDSWSFGVLLWEIFSlGYMPYPGRTN-QEVLDFVVGGGRMD- 743
Cdd:cd14025 144 ngLSHSHDLSRDGLRGTI--AYLPPERFKEKnrCPDTKHDVYSFAIVIWGILT-QKKPFAGENNiLHIMVKVVKGHRPSl 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 744 ------PPRGCPGPVyRIMTQCWQHEPELRPSFASI 773
Cdd:cd14025 221 spiprqRPSECQQMI-CLMKRCWDQDPRKRPTFQDI 255
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
516-717 4.16e-13

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: 71.19  E-value: 4.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLpeLCSPQDELdFLMEAL----IISKFRHQNIVRCVGLSLRATPRlille 591
Cdd:cd07866  16 LGEGTFGEVYKARQI-----KTGRVVALKKI--LMHNEKDG-FPITALreikILKKLKHPNVVPLIDMAVERPDK----- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 lmSGGDMKSF--------------LRHSRPHLGQPS-PLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGp 656
Cdd:cd07866  83 --SKRKRGSVymvtpymdhdlsglLENPSVKLTESQiKCYMLQLLE-------GINYLHENHILHRDIKAANILIDNQG- 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 657 srVAKIGDFGMARDIYRASY-----YRRGDRALLPV---KWM-PPEAFL-EGIFTSKTDSWSFGVLLWEIF 717
Cdd:cd07866 153 --ILKIADFGLARPYDGPPPnpkggGGGGTRKYTNLvvtRWYrPPELLLgERRYTTAVDIWGIGCVFAEMF 221
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
514-718 4.95e-13

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: 70.08  E-value: 4.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGLPGDSSPLQVAI-----KTLPELCSPQDELDFLmealiiSKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIdpintEASKEVKALECEIQLL------KNLQHERIVQYYGCLQDEKSLSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHsrphLGQPSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMA 668
Cdd:cd06625  80 FMEYMPGGSVKDEIKA----YGALTENVTR---KYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGN---VKLGDFGAS 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42544153 669 RDIYRAsyyrRGDRALLPVK----WMPPEAFLEGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd06625 150 KRLQTI----CSSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLT 199
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
516-774 7.31e-13

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: 69.61  E-value: 7.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGE-VYEGLVIGLPgdssplqVAIK-TLPELCSPQD-ELDFLMEAliiskFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd13982   9 LGYGSEGTiVFRGTFDGRP-------VAVKrLLPEFFDFADrEVQLLRES-----DEHPNVIRYFCTEKDRQFLYIALEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 M---------SGGDMKSFLRHSRphlgqpsplvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagPSRV---- 659
Cdd:cd13982  77 CaaslqdlveSPRESKLFLRPGL------------EPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIST--PNAHgnvr 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFGMAR--DIYRASYYRRGDRALlPVKWMPPEAFLEGIF---TSKTDSWSFGVLLWEIFSLGYMPYPGRTNQE--V 732
Cdd:cd13982 143 AMISDFGLCKklDVGRSSFSRRSGVAG-TSGWIAPEMLSGSTKrrqTRAVDIFSLGCVFYYVLSGGSHPFGDKLEREanI 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42544153 733 LDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd13982 222 LKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVL 263
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
498-781 9.05e-13

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 69.67  E-value: 9.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 498 LPPGVTEVSPANVTLLRALGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCV 577
Cdd:cd08229  14 LRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLL---DGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 578 GLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQ-PSPLVMRDLLQLaqdiaqgCHYLEENH---FIHRDIAARNCLLSC 653
Cdd:cd08229  91 ASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLiPEKTVWKYFVQL-------CSALEHMHsrrVMHRDIKPANVFITA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 654 AGpsrVAKIGDFGMARdiYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQ--- 730
Cdd:cd08229 164 TG---VVKLGDLGLGR--FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLysl 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 731 ----EVLDFvvgggrmdPPrgCPGPVY-----RIMTQCWQHEPELRPSFA---SILERLQYCT 781
Cdd:cd08229 239 ckkiEQCDY--------PP--LPSDHYseelrQLVNMCINPDPEKRPDITyvyDVAKRMHART 291
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
587-731 1.22e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 69.18  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMksfLRHSRPHLGQPSPlvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFG 666
Cdd:cd14198  84 ILILEYAAGGEI---FNLCVPDLAEMVS--ENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFG 158
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 667 MARDIYRASYYRrgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQE 731
Cdd:cd14198 159 MSRKIGHACELR---EIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQE 219
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
542-778 1.30e-12

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 69.35  E-value: 1.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 542 AIKTLPELCSPQDELDF---LM-EALIISKFRHQNIVRCVGLSLRATPRLILLelMSGGDMKSF-LRHSRPHLGQpSPLV 616
Cdd:cd14001  32 AVKKINSKCDKGQRSLYqerLKeEAKILKSLNHPNIVGFRAFTKSEDGSLCLA--MEYGGKSLNdLIEERYEAGL-GPFP 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 617 MRDLLQLAQDIAQGCHYLE-ENHFIHRDIAARNCLLScaGPSRVAKIGDFGMArdiyrasyyrrgdralLPVK------- 688
Cdd:cd14001 109 AATILKVALSIARALEYLHnEKKILHGDIKSGNVLIK--GDFESVKLCDFGVS----------------LPLTenlevds 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 689 -----------WMPPEAFLEG-IFTSKTDSWSFGVLLWEIFSL-------GYMPYPGRTN-------QEVLDFVVGGGRM 742
Cdd:cd14001 171 dpkaqyvgtepWKAKEALEEGgVITDKADIFAYGLVLWEMMTLsvphlnlLDIEDDDEDEsfdedeeDEEAYYGTLGTRP 250
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 743 DPPRGCPGPVYRIMTQ----CWQHEPELRPSFASILERLQ 778
Cdd:cd14001 251 ALNLGELDDSYQKVIElfyaCTQEDPKDRPSAAHIVEALE 290
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
513-791 1.60e-12

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: 69.30  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGlviglPGDSSPLQVAIKTLPELCSPQDE--LDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd06633  26 LHEIGHGSFGAVYFA-----TNSHTNEVVAIKKMSYSGKQTNEkwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVM 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 E--LMSGGDMKSFlrHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFGMA 668
Cdd:cd06633 101 EycLGSASDLLEV--HKKP-------LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT--EPGQV-KLADFGSA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYrrgdraLLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEIFSLGympyPGRTNQEVLDFVVGGGRMDPP 745
Cdd:cd06633 169 SIASPANSF------VGTPYWMAPEVILamdEGQYDGKVDIWSLGITCIELAERK----PPLFNMNAMSALYHIAQNDSP 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544153 746 ----RGCPGPVYRIMTQCWQHEPELRPSFASILeRLQYCTQD--PDVLNSLL 791
Cdd:cd06633 239 tlqsNEWTDSFRGFVDYCLQKIPQERPSSAELL-RHDFVRRErpPRVLIDLI 289
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
504-786 1.60e-12

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: 68.94  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLMEALIISK-FRHQNIVRCVGLSLR 582
Cdd:cd06618  11 KADLNDLENLGEIGSGTCGQVYKMRHK-----KTGHVMAVKQMRRSGNKEENKRILMDLDVVLKsHDCPYIVKCYGYFIT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGGDMKSFLRhsrphLGQPSPlvMRDLLQLAQDIAQGCHYLEENH-FIHRDIAARNCLLSCAGpsrVAK 661
Cdd:cd06618  86 DSDVFICMELMSTCLDKLLKR-----IQGPIP--EDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESG---NVK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARdiyRASYYRRGDRALLPVKWMPPEAFLEGIFTS---KTDSWSFGVLLWEIfSLGYMPYPG-RTNQEVLDFVV 737
Cdd:cd06618 156 LCDFGISG---RLVDSKAKTRSAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVEL-ATGQFPYRNcKTEFEVLTKIL 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 738 GggrMDPPRGCPGPVYRIMTQ-----CWQHEPELRPSFASILER---LQYCTQDPDV 786
Cdd:cd06618 232 N---EEPPSLPPNEGFSPDFCsfvdlCLTKDHRYRPKYRELLQHpfiRRYETAEVDV 285
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
517-777 1.95e-12

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: 68.62  E-value: 1.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 517 GHGAFGEVYEGLVIGLPgdssplqVAIKTLPElcspQDELDFLMEALIISK--FRHQNIVRCVGLSLRATP-RLILLELM 593
Cdd:cd13998   4 GKGRFGEVWKASLKNEP-------VAVKIFSS----RDKQSWFREKEIYRTpmLKHENILQFIAADERDTAlRTELWLVT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLRHSRPHLgqpspLVMRDLLQLAQDIAQGCHYLEENHFI---------HRDIAARNCLLSCAGpsrVAKIGD 664
Cdd:cd13998  73 AFHPNGSL*DYLSLHT-----IDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDG---TCCIAD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMArdIYRASYYRRGDRALLP----VKWMPPEAfLEGI-----FTS--KTDSWSFGVLLWEIFSL---------GYMP- 723
Cdd:cd13998 145 FGLA--VRLSPSTGEEDNANNGqvgtKRYMAPEV-LEGAinlrdFESfkRVDIYAMGLVLWEMASRctdlfgiveEYKPp 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 724 ----YPGRTNQEVLDFVVGGGRMDP--PRG---CPG--PVYRIMTQCWQHEPELRPSFASILERL 777
Cdd:cd13998 222 fyseVPNHPSFEDMQEVVVRDKQRPniPNRwlsHPGlqSLAETIEECWDHDAEARLTAQCIEERL 286
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
511-774 2.07e-12

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: 68.23  E-value: 2.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYegLVIGLPGDSsplQVAIKTLPELCSPQDELDFL-MEALIISKFRHQNIVrcvglSLRATPR--- 586
Cdd:cd08223   3 QFLRVIGKGSYGEVW--LVRHKRDRK---QYVIKKLNLKNASKRERKAAeQEAKLLSKLKHPNIV-----SYKESFEged 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 ---LILLELMSGGDMKSFLRHSRphlGQPspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIG 663
Cdd:cd08223  73 gflYIVMGFCEGGDLYTRLKEQK---GVL--LEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARdIYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVvgGGRMD 743
Cdd:cd08223 145 DLGIAR-VLESSSDMATTLIGTPY-YMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKIL--EGKLP 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 42544153 744 P-PRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd08223 221 PmPKQYSPELGELIKAMLHQDPEKRPSVKRIL 252
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
608-778 2.16e-12

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: 68.29  E-value: 2.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 608 HLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYRASyyrrGDRALLPV 687
Cdd:cd13975  92 YTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLD---KKNRAKITDLGFCKPEAMMS----GSIVGTPI 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 688 KwMPPEAFlEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQ-----EVLDFVVGGGRmdpPRGCP---GPVYRIMTQC 759
Cdd:cd13975 165 H-MAPELF-SGKYDNSVDVYAFGILFWYLCA-GHVKLPEAFEQcaskdHLWNNVRKGVR---PERLPvfdEECWNLMEAC 238
                       170
                ....*....|....*....
gi 42544153 760 WQHEPELRPSFASILERLQ 778
Cdd:cd13975 239 WSGDPSQRPLLGIVQPKLQ 257
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
516-772 2.26e-12

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: 68.16  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgDSSPLQVAIKTLPE--LCSPQDELDflMEALIISKFRHQNIVRCVGLSLRATPRLILLELM 593
Cdd:cd14120   1 IGHGAFAVVFKGRHR----KKPDLPVAIKCITKknLSKSQNLLG--KEIKILKELSHENVVALLDCQETSSSVYLVMEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLrHSRphlGQPSPLVMRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVA------KIGDFGM 667
Cdd:cd14120  75 NGGDLADYL-QAK---GTLSEDTIRVFLQ---QIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSpndirlKIADFGF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 ARdiyrasYYRRGDRALL----PVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMD 743
Cdd:cd14120 148 AR------FLQDGMMAATlcgsPM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEKNANLR 219
                       250       260       270
                ....*....|....*....|....*....|.
gi 42544153 744 P--PRGCPGPVYRIMTQCWQHEPELRPSFAS 772
Cdd:cd14120 220 PniPSGTSPALKDLLLGLLKRNPKDRIDFED 250
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
510-778 2.51e-12

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: 68.46  E-value: 2.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGlpgdssplQVAIKTLPELCSPQDELD-FLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14152   2 IELGELIGQGRWGKVHRGRWHG--------EVAIRLLEIDGNNQDHLKlFKKEVMNYRQTRHENVVLFMGACMHPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSRPHLGqpsplvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScAGPSRVAKIGDFGMA 668
Cdd:cd14152  74 ITSFCKGRTLYSFVRDPKTSLD------INKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGIS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRAsyyRRGDRALLPVKW---MPPEAFLEGI---------FTSKTDSWSFGVLLWEIFSLGYmPYPgRTNQEVLDFV 736
Cdd:cd14152 147 GVVQEG---RRENELKLPHDWlcyLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYELQARDW-PLK-NQPAEALIWQ 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 737 VGGG----RMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14152 222 IGSGegmkQVLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLE 267
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
516-775 3.87e-12

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: 67.43  E-value: 3.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELdfLMEALII-SKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd06624  16 LGKGTFGVVYAARDL-----STQVRIAIKEIPERDSREVQP--LHEEIALhSRLSHKNIVQYLGSVSEDGFFKIFMEQVP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRhsrphlGQPSPLVMRD--LLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAgpSRVAKIGDFGMARDIY 672
Cdd:cd06624  89 GGSLSALLR------SKWGPLKDNEntIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--SGVVKISDFGTSKRLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASYYRRGDRALLpvKWMPPEAFLEGI--FTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVLDFVVGGGRMDP--PRGC 748
Cdd:cd06624 161 GINPCTETFTGTL--QYMAPEVIDKGQrgYGPPADIWSLGCTIIEM-ATGKPPFIELGEPQAAMFKVGMFKIHPeiPESL 237
                       250       260
                ....*....|....*....|....*..
gi 42544153 749 PGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06624 238 SEEAKSFILRCFEPDPDKRATASDLLQ 264
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
512-713 3.94e-12

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: 67.38  E-value: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYegLVIGLpgdSSPLQVAIKTL--PELCSPQDE----LDFLMEALIISKF-RHQNIVRCVGLSLRAT 584
Cdd:cd13993   4 LISPIGEGAYGVVY--LAVDL---RTGRKYAIKCLykSGPNSKDGNdfqkLPQLREIDLHRRVsRHPNIITLHDVFETEV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHLGQPSpLVMRDLLQLAQDIAQgCHyleeNHFI-HRDIAARNCLLSCAGPSrvAKIG 663
Cdd:cd13993  79 AIYIVLEYCPNGDLFEAITENRIYVGKTE-LIKNVFLQLIDAVKH-CH----SLGIyHRDIKPENILLSQDEGT--VKLC 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 664 DFGMARDIYRASYYRRGDRallpvKWMPPEAF------LEGIFTSKTDSWSFGVLL 713
Cdd:cd13993 151 DFGLATTEKISMDFGVGSE-----FYMAPECFdevgrsLKGYPCAAGDIWSLGIIL 201
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
513-716 4.06e-12

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 68.15  E-value: 4.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYeglvigLPGDSSPLQV-AIKTLPELCSPQDE--LDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd06635  30 LREIGHGSFGAVY------FARDVRTSEVvAIKKMSYSGKQSNEkwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFGMAR 669
Cdd:cd06635 104 MEYCLGSASDLLEVHKKP-------LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT--EPGQV-KLADFGSAS 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 DIYRASYYrrgdraLLPVKWMPPEAFL---EGIFTSKTDSWSFGVLLWEI 716
Cdd:cd06635 174 IASPANSF------VGTPYWMAPEVILamdEGQYDGKVDVWSLGITCIEL 217
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
513-776 4.48e-12

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: 67.07  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGE--VYEGLviglpGDSSPL---QVAIKTLPElcspQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL 587
Cdd:cd08221   5 VRVLGRGAFGEavLYRKT-----EDNSLVvwkEVNLSRLSE----KERRDALNEIDILSLLNHDNIITYYNHFLDGESLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRPHLgQPSPLVMRDLLQLAQDIAqgchYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGM 667
Cdd:cd08221  76 IEMEYCNGGNLHDKIAQQKNQL-FPEEVVLWYLYQIVSAVS----HIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 ARDIyrASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMpyPGRTNQEVL--DFVVGGGRMDPP 745
Cdd:cd08221 148 SKVL--DSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRT--FDATNPLRLavKIVQGEYEDIDE 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 42544153 746 RGCPGpVYRIMTQCWQHEPELRPSFASILER 776
Cdd:cd08221 224 QYSEE-IIQLVHDCLHQDPEDRPTAEELLER 253
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
508-716 9.72e-12

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 66.68  E-value: 9.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 508 ANVTLLralGHGAFGEVYEGLVIGLPGdsspLQVAIKTL-PELCSPQDELDFLMEALIISKFR---HQNIVRCVGlSLRA 583
Cdd:cd14052   3 ANVELI---GSGEFSQVYKVSERVPTG----KVYAVKKLkPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLID-SWEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRL-ILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAqgchYLEENHFIHRDIAARNCLLSCAGpsrVAKI 662
Cdd:cd14052  75 HGHLyIQTELCENGSLDVFLSELGLLGRLDEFRVWKILVELSLGLR----FIHDHHFVHLDLKPANVLITFEG---TLKI 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMA------RDIyrasyYRRGDRallpvKWMPPEAFLEGIFTSKTDSWSFGVLLWEI 716
Cdd:cd14052 148 GDFGMAtvwpliRGI-----EREGDR-----EYIAPEILSEHMYDKPADIFSLGLILLEA 197
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
516-737 1.31e-11

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: 65.75  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLpELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14192  12 LGGGRFGQVHKCTEL-----STGLTLAAKII-KVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMARdiyras 675
Cdd:cd14192  86 GELFDRITDESYQLTE------LDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQI-KIIDFGLAR------ 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 676 yyRRGDRALLPVKWMPPEAFLEGI----FTS-KTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd14192 153 --RYKPREKLKVNFGTPEFLAPEVvnydFVSfPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNIV 216
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
511-719 1.33e-11

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: 66.02  E-value: 1.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgDSSPLqVAIKTL------PELCSPQDELDFLMEaliISKfrHQNIVRCVGLsLRAT 584
Cdd:cd07830   2 KVIKQLGDGTFGSVYLARNK----ETGEL-VAIKKMkkkfysWEECMNLREVKSLRK---LNE--HPNIVKLKEV-FREN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRL-ILLELMSG---GDMKSflRHSRPHlgqpSPLVMRDLLQlaQdIAQGCHYLEENHFIHRDIAARNCLLScagPSRVA 660
Cdd:cd07830  71 DELyFVFEYMEGnlyQLMKD--RKGKPF----SESVIRSIIY--Q-ILQGLAHIHKHGFFHRDLKPENLLVS---GPEVV 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 661 KIGDFGMARDI--------------YRAsyyrrgdrallpvkwmpPEAFLE-GIFTSKTDSWSFGVLLWEIFSL 719
Cdd:cd07830 139 KIADFGLAREIrsrppytdyvstrwYRA-----------------PEILLRsTSYSSPVDIWALGCIMAELYTL 195
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
514-774 1.53e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 67.59  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  514 RALGHGAFGEVyegLVIGLPGDSSPLQVAIKTLpELCSPQD------ELDFLMEALIISkfrhqnIVRCVGLSLRATPR- 586
Cdd:PTZ00283  38 RVLGSGATGTV---LCAKRVSDGEPFAVKVVDM-EGMSEADknraqaEVCCLLNCDFFS------IVKCHEDFAKKDPRn 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  587 -------LILLELMSGGDM----KSFLRHSRPHLGQPSPLVMRDLLqLAqdiaqgCHYLEENHFIHRDIAARNCLLSCAG 655
Cdd:PTZ00283 108 penvlmiALVLDYANAGDLrqeiKSRAKTNRTFREHEAGLLFIQVL-LA------VHHVHSKHMIHRDIKSANILLCSNG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  656 psrVAKIGDFGMARdIYRASYYRRGDRALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGyMPYPGRTNQEVLD 734
Cdd:PTZ00283 181 ---LVKLGDFGFSK-MYAATVSDDVGRTFCGTPyYVAPEIWRRKPYSKKADMFSLGVLLYELLTLK-RPFDGENMEEVMH 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 42544153  735 FVVgGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFASIL 774
Cdd:PTZ00283 256 KTL-AGRYDPlPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
511-733 1.70e-11

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: 65.99  E-value: 1.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKtlpelCSPQD------ELDflmealIISKFRHQNIVRCVG---LSL 581
Cdd:cd14137   7 TIEKVIGSGSFGVVYQAKLL-----ETGEVVAIK-----KVLQDkryknrELQ------IMRRLKHPNIVKLKYffySSG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 582 RATPRLIL---LELMSgGDMKSFLRHSRpHLGQPSPLVMRDLL--QLAQDIAqgchYLEENHFIHRDIAARNCLLScagP 656
Cdd:cd14137  71 EKKDEVYLnlvMEYMP-ETLYRVIRHYS-KNKQTIPIIYVKLYsyQLFRGLA----YLHSLGICHRDIKPQNLLVD---P 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 657 SR-VAKIGDFGMARDI--------YRAS-YYRrgdrallpvkwmPPEAFLeGI--FTSKTDSWSFGVLLWEIFsLGYMPY 724
Cdd:cd14137 142 ETgVLKLCDFGSAKRLvpgepnvsYICSrYYR------------APELIF-GAtdYTTAIDIWSAGCVLAELL-LGQPLF 207

                ....*....
gi 42544153 725 PGRTNQEVL 733
Cdd:cd14137 208 PGESSVDQL 216
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
514-775 3.12e-11

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: 64.89  E-value: 3.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgDSSPLQVAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd14117  12 RPLGKGKFGNVYLARE-----KQSKFIVALKVLfkSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHLGQPSPLVMRDLlqlaqdiAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMArdI 671
Cdd:cd14117  87 YAPRGELYKELQKHGRFDEQRTATFMEEL-------ADALHYCHEKKVIHRDIKPENLLMGYKGE---LKIADFGWS--V 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYYRRGDRALLpvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGp 751
Cdd:cd14117 155 HAPSLRRRTMCGTL--DYLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTETYRRIVKVDLKFPPFLSDG- 230
                       250       260
                ....*....|....*....|....
gi 42544153 752 VYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14117 231 SRDLISKLLRYHPSERLPLKGVME 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
509-724 4.09e-11

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: 64.20  E-value: 4.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLViglpGDSSPLqVAIKTLPELCSPQDELDFL-MEALIISKFRHQNIVRCvgLSLRATPR- 586
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRR----KYTGQV-VALKFIPKRGKSEKELRNLrQEIEILRKLNHPNIIEM--LDSFETKKe 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFG 666
Cdd:cd14002  75 FVVVTEYAQGELFQILEDDGT-------LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILI---GKGGVVKLCDFG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 667 MARDIYRASYyrrgdrALLPVK----WMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPY 724
Cdd:cd14002 145 FARAMSCNTL------VLTSIKgtplYMAPELVQEQPYDHTADLWSLGCILYELF-VGQPPF 199
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
561-745 4.18e-11

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: 64.28  E-value: 4.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHlgqpsplVMRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:cd14184  49 EVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFDAITSSTKY-------TERDASAMVYNLASALKYLHGLCIV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNcLLSCAGP--SRVAKIGDFGMARDIYRASYYRRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWeIFS 718
Cdd:cd14184 122 HRDIKPEN-LLVCEYPdgTKSLKLGDFGLATVVEGPLYTVCGTPT-----YVAPEIIAETGYGLKVDIWAAGVITY-ILL 194
                       170       180
                ....*....|....*....|....*...
gi 42544153 719 LGYMPYPGRTN-QEVLDFVVGGGRMDPP 745
Cdd:cd14184 195 CGFPPFRSENNlQEDLFDQILLGKLEFP 222
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
561-733 4.95e-11

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: 64.25  E-value: 4.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFlrhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:cd14195  58 EVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDF-------LAEKESLTEEEATQFLKQILDGVHYLHSKRIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNC-LLSCAGPSRVAKIGDFGMARDIYRASYYRrgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSl 719
Cdd:cd14195 131 HFDLKPENImLLDKNVPNPRIKLIDFGIAHKIEAGNEFK---NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS- 206
                       170
                ....*....|....
gi 42544153 720 GYMPYPGRTNQEVL 733
Cdd:cd14195 207 GASPFLGETKQETL 220
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
516-717 5.67e-11

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: 64.21  E-value: 5.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYE------GLVIGLpgDSSPLQVAIKTLPelCSPQDELDFLMEaliISKFRHQNIVR----CVGLSLRATP 585
Cdd:cd07863   8 IGVGAYGTVYKardphsGHFVAL--KSVRVQTNEDGLP--LSTVREVALLKR---LEAFDHPNIVRlmdvCATSRTDRET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMSGGDMKSFLRHSrPHLGQPSPLVmRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDF 665
Cdd:cd07863  81 KVTLVFEHVDQDLRTYLDKV-PPPGLPAETI-KDLMR---QFLRGLDFLHANCIVHRDLKPENILVTSGGQ---VKLADF 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544153 666 GMARdIYraSYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIF 717
Cdd:cd07863 153 GLAR-IY--SCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
516-724 1.10e-10

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: 63.10  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLpelcSPQDELDFLMEALIISKFRHQNIVRCVGlSLRATPR-----LILL 590
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKL----SKGERQRFSEEVEMLKGLQHPNIVRFYD-SWKSTVRghkciILVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENH--FIHRDIAARNCLLScaGPSRVAKIGDFGMA 668
Cdd:cd14033  84 ELMTSGTLKTYLKRFRE-------MKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFIT--GPTGSVKIGDLGLA 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 669 rDIYRASYYRrgdRALLPVKWMPPEAFLEGiFTSKTDSWSFGVLLWEIFSLGYmPY 724
Cdd:cd14033 155 -TLKRASFAK---SVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEY-PY 204
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
511-716 1.34e-10

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: 62.71  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEglvigLPGDSSPLQVAIKTLPELC-SPQDELDFLMEALIISKF-RHQNIVRCVglslRA---TP 585
Cdd:cd14050   4 TILSKLGEGSFGEVFK-----VRSREDGKLYAVKRSRSRFrGEKDRKRKLEEVERHEKLgEHPNCVRFI----KAweeKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RL-ILLELMSggdmKSFLRHSRPHLGQPSPLVMRDLLqlaqDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGD 664
Cdd:cd14050  75 ILyIQTELCD----TSLQQYCEETHSLPESEVWNILL----DLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKLGD 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42544153 665 FGMARDIYRA--SYYRRGDRallpvKWMPPEAfLEGIFTSKTDSWSFGVLLWEI 716
Cdd:cd14050 144 FGLVVELDKEdiHDAQEGDP-----RYMAPEL-LQGSFTKAADIFSLGITILEL 191
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
522-724 1.52e-10

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: 63.08  E-value: 1.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 522 GEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFlMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSF 601
Cdd:cd06659  30 GEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLF-NEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 602 LRHSRphlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsRVaKIGDFGMARDIYRASYYRRgd 681
Cdd:cd06659 109 VSQTR--------LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG--RV-KLSDFGFCAQISKDVPKRK-- 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42544153 682 rALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd06659 176 -SLVGTPyWMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPY 217
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
516-769 1.64e-10

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: 63.06  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLvigLPGDSsplqVAIKTLPELcspqDELDFLMEALIISK--FRHQNIVRCVGLSLRAT---PRLILL 590
Cdd:cd14056   3 IGKGRYGEVWLGK---YRGEK----VAVKIFSSR----DEDSWFRETEIYQTvmLRHENILGFIAADIKSTgswTQLWLI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 -ELMSGGDMKSFLrhsrphlgQPSPLVMRDLLQLAQDIAQG-CHYLEENHFI-------HRDIAARNCL----LSCAgps 657
Cdd:cd14056  72 tEYHEHGSLYDYL--------QRNTLDTEEALRLAYSAASGlAHLHTEIVGTqgkpaiaHRDLKSKNILvkrdGTCC--- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 rvakIGDFGMArdiyrASYYRRGDRALLPV-------KWMPPEAFLEGI----FTS--KTDSWSFGVLLWEI-------- 716
Cdd:cd14056 141 ----IADLGLA-----VRYDSDTNTIDIPPnprvgtkRYMAPEVLDDSInpksFESfkMADIYSFGLVLWEIarrceigg 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 717 FSLGYM-PYPGR-----TNQEVLDFVVGGGRMD--PPRGCPGPVYR----IMTQCWQHEPELRPS 769
Cdd:cd14056 212 IAEEYQlPYFGMvpsdpSFEEMRKVVCVEKLRPpiPNRWKSDPVLRsmvkLMQECWSENPHARLT 276
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
516-669 1.77e-10

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: 62.88  E-value: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGlvIGLPGDSsplQVAIKTLPeLCSPQDEL--DFLMEALIISKFRHQNIVRCvgLSLRATPRLILL--E 591
Cdd:cd07829   7 LGEGTYGVVYKA--KDKKTGE---IVALKKIR-LDNEEEGIpsTALREISLLKELKHPNIVKL--LDVIHTENKLYLvfE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGgDMKSFLRHSRPHLgqPSPLV---MRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMA 668
Cdd:cd07829  79 YCDQ-DLKKYLDKRPGPL--PPNLIksiMYQLLR-------GLAYCHSHRILHRDLKPQNLLINRDG---VLKLADFGLA 145

                .
gi 42544153 669 R 669
Cdd:cd07829 146 R 146
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
516-775 1.84e-10

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: 62.24  E-value: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglpgDS-SPLQVA-----IKTLPelcsPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd13983   9 LGRGSFKTVYRAF------DTeEGIEVAwneikLRKLP----KAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 L--ELMSGGDMKSFLRHsrphLGQPSPLVMRdllQLAQDIAQGCHYLeenH-----FIHRDIAARNCLLScaGPSRVAKI 662
Cdd:cd13983  79 FitELMTSGTLKQYLKR----FKRLKLKVIK---SWCRQILEGLNYL---HtrdppIIHRDLKCDNIFIN--GNTGEVKI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMA---RDIYRASyyrrgdrallpV----KWMPPEAFLEGiFTSKTDSWSFGVLLWEIFSLGYmPYPGRTN-QEVLD 734
Cdd:cd13983 147 GDLGLAtllRQSFAKS-----------VigtpEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEY-PYSECTNaAQIYK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42544153 735 FVVGGgrmDPPRG---CPGP-VYRIMTQCWQHePELRPSFASILE 775
Cdd:cd13983 214 KVTSG---IKPESlskVKDPeLKDFIEKCLKP-PDERPSARELLE 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
588-784 2.06e-10

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: 62.31  E-value: 2.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRpHLgqPSPLVMRdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGM 667
Cdd:cd14010  71 LVVEYCTGGDLETLLRQDG-NL--PESSVRK----FGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNG---TLKLSDFGL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 AR------DIYRASYYRRGDRALLPVK--------WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14010 141 ARregeilKELFGQFSDEGNVNKVSKKqakrgtpyYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFVAESFTELV 219
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42544153 734 DFVVGGgrmDPPRgcpgpvyriMTQCWQHEPElrPSFASILERLqyCTQDP 784
Cdd:cd14010 220 EKILNE---DPPP---------PPPKVSSKPS--PDFKSLLKGL--LEKDP 254
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
516-821 2.22e-10

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: 62.54  E-value: 2.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglpgdsSPLQVAIKTLPElcspQDELD-------FLMEALIISKFRHQNIVRCVGLSL-RATPRL 587
Cdd:cd14159   1 IGEGGFGCVYQAVM-------RNTEYAVKRLKE----DSELDwsvvknsFLTEVEKLSRFRHPNIVDLAGYSAqQGNYCL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGgdmkSFLRHSRPHLGQPsPLVMRDLLQLAQDIAQGCHYLEENH--FIHRDIAARNCLLscaGPSRVAKIGDF 665
Cdd:cd14159  70 IYVYLPNG----SLEDRLHCQVSCP-CLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILL---DAALNPKLGDF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 666 GMARDIYRA------SYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlgympypGRTNQEVldfvvgg 739
Cdd:cd14159 142 GLARFSRRPkqpgmsSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT-------GRRAMEV------- 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 740 grmdppRGCPGPVYRI----MTQCWQHEPELRPSFASilerLQYCTQDPDVLNSLLPMELGPTPeEEGTSGLGNRSLECL 815
Cdd:cd14159 208 ------DSCSPTKYLKdlvkEEEEAQHTPTTMTHSAE----AQAAQLATSICQKHLDPQAGPCP-PELGIEISQLACRCL 276
                       330
                ....*....|..
gi 42544153 816 ------RPPQPQ 821
Cdd:cd14159 277 hrrakkRPPMTE 288
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
506-718 2.37e-10

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: 62.41  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 506 SPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKtlPELCSPQDELDFL-MEALIISKFRHQNIVRCVG-LSLRA 583
Cdd:cd06651   5 APINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFD--PESPETSKEVSALeCEIQLLKNLQHERIVQYYGcLRDRA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRL-ILLELMSGGDMKSFLRHsrphLGQPSPLVMRdllQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKI 662
Cdd:cd06651  83 EKTLtIFMEYMPGGSVKDQLKA----YGALTESVTR---KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKL 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 663 GDFGMARDIYRASYYRRGDRALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd06651 153 GDFGASKRLQTICMSGTGIRSVTGTPyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 209
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
516-733 2.56e-10

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: 61.90  E-value: 2.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglpGDSSPLQVAIKTLPELCSPQDELdfLMEALIISKFRHQNIVrcvGL--SLRATPRLIL-LEL 592
Cdd:cd14006   1 LGRGRFGVVKRCI-----EKATGREFAAKFIPKRDKKKEAV--LREISILNQLQHPRII---QLheAYESPTELVLiLEL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHSRPHLGQPSPLVMRDLLqlaqdiaQGCHYLEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMARDIY 672
Cdd:cd14006  71 CSGGELLDRLAERGSLSEEEVRTYMRQLL-------EGLQYLHNHHILHLDLKPENILLADRPSPQI-KIIDFGLARKLN 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 673 RASYYRRGDRALlpvKWMPPEAFL-EGIFTSkTDSWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14006 143 PGEELKEIFGTP---EFVAPEIVNgEPVSLA-TDMWSIGVLTYVLLS-GLSPFLGEDDQETL 199
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
560-739 2.78e-10

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: 61.96  E-value: 2.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 560 MEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMksFlrhsrPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHF 639
Cdd:cd14095  47 NEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGGDL--F-----DAITSSTKFTERDASRMVTDLAQALKYLHSLSI 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 640 IHRDIAARNcLLSCAGP--SRVAKIGDFGMARDIyrasyyrrgDRALLPVKWMP----PEAFLEGIFTSKTDSWSFGVLL 713
Cdd:cd14095 120 VHRDIKPEN-LLVVEHEdgSKSLKLADFGLATEV---------KEPLFTVCGTPtyvaPEILAETGYGLKVDIWAAGVIT 189
                       170       180
                ....*....|....*....|....*...
gi 42544153 714 WeIFSLGYMPY--PGRTNQEVLDFVVGG 739
Cdd:cd14095 190 Y-ILLCGFPPFrsPDRDQEELFDLILAG 216
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
516-732 2.92e-10

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: 61.76  E-value: 2.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYegLVIglpgDSSPLQV-AIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVgLSLRATPRLIL-LE 591
Cdd:cd05123   1 LGKGSFGKVL--LVR----KKDTGKLyAMKVLrkKEIIKRKEVEHTLNERNILERVNHPFIVKLH-YAFQTEEKLYLvLD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHsRPHLGQpsplvmrDLLQL-AQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARD 670
Cdd:cd05123  74 YVPGGELFSHLSK-EGRFPE-------ERARFyAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH---IKLTDFGLAKE 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 671 IYRasyyrRGDRALLPV---KWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEV 732
Cdd:cd05123 143 LSS-----DGDRTYTFCgtpEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEI 201
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
511-714 3.01e-10

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: 62.57  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLViglpgDSSPLQVAIKTLpELCSPQDELDFLME--ALIISKFRHQNIVR---CV----GLSL 581
Cdd:cd13977   3 SLIREVGRGSYGVVYEAVV-----RRTGARVAVKKI-RCNAPENVELALREfwALSSIQRQHPNVIQleeCVlqrdGLAQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 582 RAT------------------------PR-----LILLELMSGGDMKSFLRHSRPHLGQPSPLvmrdLLQLAQDIAqgch 632
Cdd:cd13977  77 RMShgssksdlylllvetslkgercfdPRsacylWFVMEFCDGGDMNEYLLSRRPDRQTNTSF----MLQLSSALA---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 633 YLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARdIYRASYYRRGDRALLPVKW----------MPPEAFlEGIFTS 702
Cdd:cd13977 149 FLHRNQIVHRDLKPDNILISHKRGEPILKVADFGLSK-VCSGSGLNPEEPANVNKHFlssacgsdfyMAPEVW-EGHYTA 226
                       250
                ....*....|..
gi 42544153 703 KTDSWSFGVLLW 714
Cdd:cd13977 227 KADIFALGIIIW 238
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
515-739 3.26e-10

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: 61.47  E-value: 3.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 515 ALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPELcSPQDELDFLMEALIISKFRHQNIVRCvgLSLRATPRLILL--EL 592
Cdd:cd14190  11 VLGGGKFGKVHTCT-----EKRTGLKLAAKVINKQ-NSKDKEMVLLEIQVMNQLNHRNLIQL--YEAIETPNEIVLfmEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMksFLRHsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLsCAGPSRVAKIGDFGMARdiy 672
Cdd:cd14190  83 VEGGEL--FERI----VDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILC-VNRTGHQVKIIDFGLAR--- 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 673 rasyyRRGDRALLPVKWMPPEaFLE------GIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd14190 153 -----RYNPREKLKVNFGTPE-FLSpevvnyDQVSFPTDMWSMGVITYMLLS-GLSPFLGDDDTETLNNVLMG 218
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
561-739 3.49e-10

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: 61.73  E-value: 3.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFlrhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:cd14105  58 EVSILRQVLHPNIITLHDVFENKTDVVLILELVAGGELFDF-------LAEKESLSEEEATEFLKQILDGVNYLHTKNIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNCLL--SCAGPSRVaKIGDFGMARDIYRASYYRrgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd14105 131 HFDLKPENIMLldKNVPIPRI-KLIDFGLAHKIEDGNEFK---NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS 206
                       170       180
                ....*....|....*....|.
gi 42544153 719 lGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd14105 207 -GASPFLGDTKQETLANITAV 226
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
623-773 3.55e-10

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D 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: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 61.65  E-value: 3.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 623 LAQDIAQGCHYLEENHFIHRDIAARNCLLScagpSR-VAKIGDFGMArDIYRASYYRRGDRALLPVKWMPPE----AFLE 697
Cdd:cd14043 102 LLLDLIKGMRYLHHRGIVHGRLKSRNCVVD----GRfVLKITDYGYN-EILEAQNLPLPEPAPEELLWTAPEllrdPRLE 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 698 GIFTSKTDSWSFGVLLWEIFSLGyMPYP--GRTNQEVLDFVvgggrMDPPRGC---------PGPVYRIMTQCWQHEPEL 766
Cdd:cd14043 177 RRGTFPGDVFSFAIIMQEVIVRG-APYCmlGLSPEEIIEKV-----RSPPPLCrpsvsmdqaPLECIQLMKQCWSEAPER 250

                ....*..
gi 42544153 767 RPSFASI 773
Cdd:cd14043 251 RPTFDQI 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
507-711 3.91e-10

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: 61.55  E-value: 3.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PAN-VTLLRALGHGAFGEVYEGLviglpgDSSPLQ-VAIKTLPELCSPQDELdfLMEALIISKF-RHQNIVRCVGLSLRA 583
Cdd:cd06608   4 PAGiFELVEVIGEGTYGKVYKAR------HKKTGQlAAIKIMDIIEDEEEEI--KLEINILRKFsNHPNIATFYGAFIKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 TPRL------ILLELMSGG---DM-KSFLRHSRPhlgQPSPLVMRDLlqlaQDIAQGCHYLEENHFIHRDIAARNCLLSC 653
Cdd:cd06608  76 DPPGgddqlwLVMEYCGGGsvtDLvKGLRKKGKR---LKEEWIAYIL----RETLRGLAYLHENKVIHRDIKGQNILLTE 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 654 AGpsRVaKIGDFGMARDIYRASyYRRGDRALLPVkWMPPEAF-----LEGIFTSKTDSWSFGV 711
Cdd:cd06608 149 EA--EV-KLVDFGVSAQLDSTL-GRRNTFIGTPY-WMAPEVIacdqqPDASYDARCDVWSLGI 206
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
511-738 4.84e-10

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: 61.77  E-value: 4.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLviglpgDS-SPLQVAIKTLPELCspQDELD---FLMEALIISKFRHQNIVRCVGLsLRATPR 586
Cdd:cd07834   3 ELLKPIGSGAYGVVCSAY------DKrTGRKVAIKKISNVF--DDLIDakrILREIKILRHLKHENIIGLLDI-LRPPSP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 L------ILLELMsGGDMKSFLRHSRPhlgqpsplvmrdllqLAQDIAQ--------GCHYLEENHFIHRDIAARNCLL- 651
Cdd:cd07834  74 EefndvyIVTELM-ETDLHKVIKSPQP---------------LTDDHIQyflyqilrGLKYLHSAGVIHRDLKPSNILVn 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 -SCagpsrVAKIGDFGMARDI-----------YRAS-YYRrgdrallpvkwmPPEAFLEGI-FTSKTDSWSFGVLLWEIF 717
Cdd:cd07834 138 sNC-----DLKICDFGLARGVdpdedkgflteYVVTrWYR------------APELLLSSKkYTKAIDIWSVGCIFAELL 200
                       250       260
                ....*....|....*....|.
gi 42544153 718 sLGYMPYPGRTNQEVLDFVVG 738
Cdd:cd07834 201 -TRKPLFPGRDYIDQLNLIVE 220
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
511-715 4.95e-10

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 61.43  E-value: 4.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKT--LPELCSPQDELDF--LMEALIISKFRHQNIVRCV-------GL 579
Cdd:cd07841   3 EKGKKLGEGTYAVVYKARDK-----ETGRIVAIKKikLGERKEAKDGINFtaLREIKLLQELKHPNIIGLLdvfghksNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 580 SLratprliLLELMSGgDMKSFLRHSRPHLGQPsplvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrV 659
Cdd:cd07841  78 NL-------VFEFMET-DLEKVIKDKSIVLTPA------DIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDG---V 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFGMARD------------IYRasYYRrgdrallpvkwmPPEAFLeG--IFTSKTDSWSFGVLLWE 715
Cdd:cd07841 141 LKLADFGLARSfgspnrkmthqvVTR--WYR------------APELLF-GarHYGVGVDMWSVGCIFAE 195
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
516-724 5.01e-10

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: 61.20  E-value: 5.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVyeglVIGLPGDSSPLqVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14167  11 LGTGAFSEV----VLAEEKRTQKL-VAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMksFLRhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRAS 675
Cdd:cd14167  86 GEL--FDR-----IVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSGS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42544153 676 YYrrgDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14167 159 VM---STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 203
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
561-820 5.86e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 61.76  E-value: 5.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSflrhsrPHLGQPsplvmRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:PLN00034 122 EIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEG------THIADE-----QFLADVARQILSGIAYLHRRHIV 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  641 HRDIAARNCLLSCAgpsRVAKIGDFGMARDIyrASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDS-----WSFGVLLWE 715
Cdd:PLN00034 191 HRDIKPSNLLINSA---KNVKIADFGVSRIL--AQTMDPCNSSVGTIAYMSPERINTDLNHGAYDGyagdiWSLGVSILE 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  716 iFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCP--GPVYR-IMTQCWQHEPELRPSFASILERlqyctqdpdvlnsllP 792
Cdd:PLN00034 266 -FYLGRFPFGVGRQGDWASLMCAICMSQPPEAPAtaSREFRhFISCCLQREPAKRWSAMQLLQH---------------P 329
                        250       260
                 ....*....|....*....|....*...
gi 42544153  793 MELGPTPEEegtsGLGNRSLECLRPPQP 820
Cdd:PLN00034 330 FILRAQPGQ----GQGGPNLHQLLPPPR 353
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
557-778 5.87e-10

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: 61.13  E-value: 5.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 557 DFLMEALIISKFRHQNIVRCVGLSLRatPRLILLELMSGGDMKSFLrhSRPHLGQP-SPLVMRDLLQLAQDIAQGCHYLE 635
Cdd:cd14067  56 EFRQEASMLHSLQHPCIVYLIGISIH--PLCFALELAPLGSLNTVL--EENHKGSSfMPLGHMLTFKIAYQIAAGLAYLH 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 636 ENHFIHRDIAARNCLL-SCAGPSRV-AKIGDFGMARDIYRasyyrrgdRALLPVKWMP----PEAFLEGIFTSKTDSWSF 709
Cdd:cd14067 132 KKNIIFCDLKSDNILVwSLDVQEHInIKLSDYGISRQSFH--------EGALGVEGTPgyqaPEIRPRIVYDEKVDMFSY 203
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 710 GVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRmdPPRGCPGPV--YR---IMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14067 204 GMVLYELLS-GQRPSLGHHQLQIAKKLSKGIR--PVLGQPEEVqfFRlqaLMMECWDTKPEKRPLACSVVEQMK 274
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
541-777 6.57e-10

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


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 61.07  E-value: 6.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 541 VAIKTLPElcsPQDELD--FLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLgqpsplvmr 618
Cdd:cd14042  33 VAIKKVNK---KRIDLTreVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDILENEDIKL--------- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 619 D---LLQLAQDIAQGCHYLEENHFI-HRDIAARNCLLScagpSR-VAKIGDFGMA-------RDIYRASYYRRgdraLLp 686
Cdd:cd14042 101 DwmfRYSLIHDIVKGMHYLHDSEIKsHGNLKSSNCVVD----SRfVLKITDFGLHsfrsgqePPDDSHAYYAK----LL- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 687 vkWMPPEAFLEGIF----TSKTDSWSFGVLLWEIFslgympypgrTNQEVldFVVGGGRMDP-------PRGCPGPVYR- 754
Cdd:cd14042 172 --WTAPELLRDPNPpppgTQKGDVYSFGIILQEIA----------TRQGP--FYEEGPDLSPkeiikkkVRNGEKPPFRp 237
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 755 -------------IMTQCWQHEPELRPSFASILERL 777
Cdd:cd14042 238 sldelecpdevlsLMQRCWAEDPEERPDFSTLRNKL 273
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
624-773 6.73e-10

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 60.64  E-value: 6.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 624 AQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMArdIYR-------ASYYRRGDRALlpvkWMPPEAFL 696
Cdd:cd14045 109 ATDIARGMAYLHQHKIYHGRLKSSNCVID---DRWVCKIADYGLT--TYRkedgsenASGYQQRLMQV----YLPPENHS 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 697 EGIF--TSKTDSWSFGVLLWEIFSLG-YMPYPGRTNQEVL-----DFVVGGGRMDPPrgCPGPVYRIMTQCWQHEPELRP 768
Cdd:cd14045 180 NTDTepTQATDVYSYAIILLEIATRNdPVPEDDYSLDEAWcpplpELISGKTENSCP--CPADYVELIRRCRKNNPAQRP 257

                ....*
gi 42544153 769 SFASI 773
Cdd:cd14045 258 TFEQI 262
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
522-716 6.87e-10

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: 60.53  E-value: 6.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 522 GEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFlMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSF 601
Cdd:cd06648  16 GEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLF-NEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 602 LRHSRPHLGQPSPLVMRDLLQLAqdiaqgchYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRASYYRRgd 681
Cdd:cd06648  95 VTHTRMNEEQIATVCRAVLKALS--------FLHSQGVIHRDIKSDSILLTSDG---RVKLSDFGFCAQVSKEVPRRK-- 161
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42544153 682 rALLPVK-WMPPEAFLEGIFTSKTDSWSFGVLLWEI 716
Cdd:cd06648 162 -SLVGTPyWMAPEVISRLPYGTEVDIWSLGIMVIEM 196
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
561-733 7.76e-10

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: 60.74  E-value: 7.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFlrhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:cd14196  58 EVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDF-------LAQKESLSEEEATSFIKQILDGVNYLHTKKIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNC-LLSCAGPSRVAKIGDFGMARDIYRASYYRrgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSl 719
Cdd:cd14196 131 HFDLKPENImLLDKNIPIPHIKLIDFGLAHEIEDGVEFK---NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS- 206
                       170
                ....*....|....
gi 42544153 720 GYMPYPGRTNQEVL 733
Cdd:cd14196 207 GASPFLGDTKQETL 220
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
504-788 8.19e-10

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 60.84  E-value: 8.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 504 EVSPANVTLLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRH-QNIVRCVGLSLR 582
Cdd:cd06616   2 EFTAEDLKDLGEIGRGAFGTVNKML-----HKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDcPYIVKFYGALFR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGgDMKSFLRhsRPHLGQPSPLVMRDLLQLAQDIAQGCHYL-EENHFIHRDIAARNCLLSCAGPsrvAK 661
Cdd:cd06616  77 EGDCWICMELMDI-SLDKFYK--YVYEVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGN---IK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRaSYYRRGDRALLPvkWMPPE-----AFLEGiFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQ-EVLDF 735
Cdd:cd06616 151 LCDFGISGQLVD-SIAKTRDAGCRP--YMAPEridpsASRDG-YDVRSDVWSLGITLYEV-ATGKFPYPKWNSVfDQLTQ 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 736 VVGGgrmDPPRGCPGPVY-------RIMTQCWQHEPELRPSFASILER---LQYCTQDPDVLN 788
Cdd:cd06616 226 VVKG---DPPILSNSEERefspsfvNFVNLCLIKDESKRPKYKELLKHpfiKMYEERNVDVAA 285
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
511-778 9.54e-10

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: 60.39  E-value: 9.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYegLVIGLpgdSSPLQVAIKTLpeLCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLR-----AT 584
Cdd:cd13986   3 RIQRLLGEGGFSFVY--LVEDL---STGRLYALKKI--LCHSKEDVKEAMrEIENYRLFNHPNILRLLDSQIVkeaggKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHlGQPSPLvmRDLLQLAQDIAQGCHYLEENH---FIHRDIAARNCLLScagPSRVAK 661
Cdd:cd13986  76 EVYLLLPYYKRGSLQDEIERRLVK-GTFFPE--DRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLS---EDDEPI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRASYYRR---------GDRALLPvkWMPPEAF---LEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTN 729
Cdd:cd13986 150 LMDLGSMNPARIEIEGRRealalqdwaAEHCTMP--YRAPELFdvkSHCTIDEKTDIWSLGCTLYALM-YGESPFERIFQ 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544153 730 Q-EVLDFVVGGGRMDPPRGC--PGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd13986 227 KgDSLALAVLSGNYSFPDNSrySEELHQLVKSMLVVNPAERPSIDDLLSRVH 278
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
513-719 1.02e-09

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: 60.13  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVY-------EGLVIglpgdssplqvaIKTLP-ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd08220   5 IRVVGRGAYGTVYlcrrkddNKLVI------------IKQIPvEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHLgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVAKIGD 664
Cdd:cd08220  73 ALMIVMEYAPGGTLFEYIQQRKGSL-----LSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLN--KKRTVVKIGD 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 665 FGMARDIYRASyyrrgdRALLPVK---WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL 719
Cdd:cd08220 146 FGISKILSSKS------KAYTVVGtpcYISPELCEGKPYNQKSDIWALGCVLYELASL 197
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
588-731 1.05e-09

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 60.06  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLrHSRPHLGQPsplvmrDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGM 667
Cdd:cd14106  85 LILELAAGGELQTLL-DEEECLTEA------DVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGI 157
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 668 ARDIYRASYYRrgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQE 731
Cdd:cd14106 158 SRVIGEGEEIR---EILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDKQE 217
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
511-738 1.13e-09

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: 60.42  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKtlpELCSPQDELDFLMEALIISKF-----RHQNIVRCVGLSLRATP 585
Cdd:cd07832   3 KILGRIGEGAHGIVFKAKDR-----ETGETVALK---KVALRKLEGGIPNQALREIKAlqacqGHPYVVKLRDVFPHGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMsGGDMKSFLRHSRPHLGQPS-PLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGD 664
Cdd:cd07832  75 FVLVFEYM-LSSLSEVLRDEERPLTEAQvKRYMRMLLK-------GVAYMHANRIMHRDLKPANLLISSTG---VLKIAD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMAR----DIYRASYYRRGDRallpvkW-MPPEaFLEGI--FTSKTDSWSFGVLLWEIfsLGYMP-YPGRTNQEVLDFV 736
Cdd:cd07832 144 FGLARlfseEDPRLYSHQVATR------WyRAPE-LLYGSrkYDEGVDLWAVGCIFAEL--LNGSPlFPGENDIEQLAIV 214

                ..
gi 42544153 737 VG 738
Cdd:cd07832 215 LR 216
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
509-719 1.22e-09

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: 59.98  E-value: 1.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEG--LVIGLPgdssplqVAIKTLP--ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRArcLLDGRL-------VALKKVQifEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHlGQPSPlvMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGD 664
Cdd:cd08224  74 ELNIVLELADAGDLSRLIKHFKKQ-KRLIP--ERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANG---VVKLGD 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 665 FGMARdiYRAS------------YYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIFSL 719
Cdd:cd08224 148 LGLGR--FFSSkttaahslvgtpYY------------MSPERIREQGYDFKSDIWSLGCLLYEMAAL 200
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
516-724 1.37e-09

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: 60.12  E-value: 1.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglpGDSSPLQVAIKTLPEL-CSPQDELDFLMEALIISKFRHQNIVRCVGL--SLRATPRLILL-- 590
Cdd:cd14031  18 LGRGAFKTVYKGL-----DTETWVEVAWCELQDRkLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSweSVLKGKKCIVLvt 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPHlgqpSPLVMRdllQLAQDIAQGCHYLEENH--FIHRDIAARNCLLScaGPSRVAKIGDFGMA 668
Cdd:cd14031  93 ELMTSGTLKTYLKRFKVM----KPKVLR---SWCRQILKGLQFLHTRTppIIHRDLKCDNIFIT--GPTGSVKIGDLGLA 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 669 rDIYRASYYRrgdRALLPVKWMPPEAFLEGiFTSKTDSWSFGVLLWEIFSLGYmPY 724
Cdd:cd14031 164 -TLMRTSFAK---SVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEY-PY 213
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
512-719 2.07e-09

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: 59.59  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLMEALIISKFR-HQNIVRCVGLSL-RATPRLIL 589
Cdd:cd07831   3 ILGKIGEGTFSEVLKAQSR-----KTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLFdRKTGRLAL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 -LELMsggDMK--SFLRHSRPHLGQPSplVMRDLLQLAQdiaqGCHYLEENHFIHRDIAARNCLLScagpSRVAKIGDFG 666
Cdd:cd07831  78 vFELM---DMNlyELIKGRKRPLPEKR--VKNYMYQLLK----SLDHMHRNGIFHRDIKPENILIK----DDILKLADFG 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 667 MARDIYRASYYrrgdRALLPVKWM-PPEAFL-EGIFTSKTDSWSFGVLLWEIFSL 719
Cdd:cd07831 145 SCRGIYSKPPY----TEYISTRWYrAPECLLtDGYYGPKMDIWAVGCVFFEILSL 195
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
516-724 2.57e-09

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: 58.94  E-value: 2.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELcspqDELDFLMEALIISKFRHQNIVRCVGL--SLRATPRLILL--E 591
Cdd:cd14032   9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKV----ERQRFKEEAEMLKGLQHPNIVRFYDFweSCAKGKRCIVLvtE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHlgqpSPLVMRdllQLAQDIAQGCHYLEENH--FIHRDIAARNCLLScaGPSRVAKIGDFGMAr 669
Cdd:cd14032  85 LMTSGTLKTYLKRFKVM----KPKVLR---SWCRQILKGLLFLHTRTppIIHRDLKCDNIFIT--GPTGSVKIGDLGLA- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 670 DIYRASYYRrgdRALLPVKWMPPEAFLEGiFTSKTDSWSFGVLLWEIFSLGYmPY 724
Cdd:cd14032 155 TLKRASFAK---SVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEY-PY 204
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
570-727 2.93e-09

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: 59.27  E-value: 2.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 570 HQNIVRCVGLSLRATPRLILLELMSGGDMKSFLrHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNC 649
Cdd:cd14173  59 HRNVLELIEFFEEEDKFYLVFEKMRGGSILSHI-HRRRHFNE------LEASVVVQDIASALDFLHNKGIAHRDLKPENI 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 650 LlsCAGPSRVA--KIGDFGMARDIYRASYYR--RGDRALLP---VKWMPP---EAFLE--GIFTSKTDSWSFGVLLWEIF 717
Cdd:cd14173 132 L--CEHPNQVSpvKICDFDLGSGIKLNSDCSpiSTPELLTPcgsAEYMAPevvEAFNEeaSIYDKRCDLWSLGVILYIML 209
                       170
                ....*....|
gi 42544153 718 SlGYMPYPGR 727
Cdd:cd14173 210 S-GYPPFVGR 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
516-769 3.01e-09

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: 59.12  E-value: 3.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd06619   9 LGHGNGGTVYKAYHL-----LTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHLGQpsplvmrdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDIYR-- 673
Cdd:cd06619  84 GSLDVYRKIPEHVLGR-----------IAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQ---VKLCDFGVSTQLVNsi 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 674 ASYYRrGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPG-RTNQ------EVLDFVVgggRMDPPR 746
Cdd:cd06619 150 AKTYV-GTNA-----YMAPERISGEQYGIHSDVWSLGISFMEL-ALGRFPYPQiQKNQgslmplQLLQCIV---DEDPPV 219
                       250       260
                ....*....|....*....|....*..
gi 42544153 747 GCPG----PVYRIMTQCWQHEPELRPS 769
Cdd:cd06619 220 LPVGqfseKFVHFITQCMRKQPKERPA 246
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
509-778 3.02e-09

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: 58.88  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLpeLCSPQDELDFLMEALIISK--FRHQNIVR-CVGLSLRATP 585
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVN-----TGRRYALKRM--YFNDEEQLRVAIKEIEIMKrlCGHPNIVQyYDSAILSSEG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMS--GGDMKSFLRhSRPhlgqPSPLVMRDLLQLAQDIAQGCHYLEENH--FIHRDIAARNCLLSCAGPsrvAK 661
Cdd:cd13985  74 RKEVLLLMEycPGSLVDILE-KSP----PSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR---FK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMARDIYRAsYYRRGDRALLPVKW--------MPPEA---FLEGIFTSKTDSWSFGVLLweiFSLGYMPYPGRTNq 730
Cdd:cd13985 146 LCDFGSATTEHYP-LERAEEVNIIEEEIqknttpmyRAPEMidlYSKKPIGEKADIWALGCLL---YKLCFFKLPFDES- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42544153 731 EVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd13985 221 SKLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIIT 268
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
513-734 3.15e-09

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: 58.83  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVY------EGLVIGLPGDSSPLQ---VAIKTLPELCspqdeldfLMEALiiSKFRHQNIVR----CVGL 579
Cdd:cd07838   4 VAEIGEGAYGTVYkardlqDGRFVALKKVRVPLSeegIPLSTIREIA--------LLKQL--ESFEHPNVVRlldvCHGP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 580 SL-RATPRLILLELMSGgDMKSFLRHSrPHLGQPSPLVmRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsR 658
Cdd:cd07838  74 RTdRELKLTLVFEHVDQ-DLATYLDKC-PKPGLPPETI-KDLMR---QLLRGLDFLHSHRIVHRDLKPQNILVTSDG--Q 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 659 VaKIGDFGMARdIYraSYYRrgdrALLPVK---WM-PPEAFLEGIFTSKTDSWSFGVLLWEIFSLgyMP-YPGRTNQEVL 733
Cdd:cd07838 146 V-KLADFGLAR-IY--SFEM----ALTSVVvtlWYrAPEVLLQSSYATPVDMWSVGCIFAELFNR--RPlFRGSSEADQL 215

                .
gi 42544153 734 D 734
Cdd:cd07838 216 G 216
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
559-734 3.44e-09

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: 58.77  E-value: 3.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 559 LMEALIISKFRHQNIVR----CVGLSLRATprLILLELMSGgDMKSFLRHSRPHLGQPSplVMRDLLQLAQdiaqGCHYL 634
Cdd:cd07843  52 LREINILLKLQHPNIVTvkevVVGSNLDKI--YMVMEYVEH-DLKSLMETMKQPFLQSE--VKCLMLQLLS----GVAHL 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 635 EENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARdiyrasyyRRGDrallPVKWM----------PPEAFL-EGIFTSK 703
Cdd:cd07843 123 HDNWILHRDLKTSNLLLNNRG---ILKICDFGLAR--------EYGS----PLKPYtqlvvtlwyrAPELLLgAKEYSTA 187
                       170       180       190
                ....*....|....*....|....*....|.
gi 42544153 704 TDSWSFGVLLWEIFSLGYMpYPGRTNQEVLD 734
Cdd:cd07843 188 IDMWSVGCIFAELLTKKPL-FPGKSEIDQLN 217
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
514-745 3.56e-09

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: 58.47  E-value: 3.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELM 593
Cdd:cd14183  12 RTIGDGNFAVVKECV-----ERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMKSFLRHSRPHlgqpsplVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL-SCAGPSRVAKIGDFGMARDIY 672
Cdd:cd14183  87 KGGDLFDAITSTNKY-------TERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLATVVD 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 673 RASYYRRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPYPGRT-NQEVLDFVVGGGRMDPP 745
Cdd:cd14183 160 GPLYTVCGTPT-----YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRGSGdDQEVLFDQILMGQVDFP 227
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
555-713 3.84e-09

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: 58.14  E-value: 3.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 555 ELDFLMEALIisKFRHQNIVRCVGLSLRATPRL------ILLELMSGGDMKSFLRHSRPhlgqpSPL-----VMRDLLQl 623
Cdd:cd14012  44 LLEKELESLK--KLRHPNLVSYLAFSIERRGRSdgwkvyLLTEYAPGGSLSELLDSVGS-----VPLdtarrWTLQLLE- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 624 aqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIyRASYYRRGDRALLPVKWMPPEAFLEGI-FTS 702
Cdd:cd14012 116 ------ALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKTL-LDMCSRGSLDEFKQTYWLPPELAQGSKsPTR 188
                       170
                ....*....|.
gi 42544153 703 KTDSWSFGVLL 713
Cdd:cd14012 189 KTDVWDLGLLF 199
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
516-737 3.91e-09

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: 58.39  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEglvigLPGDSSPLQVAIKTLPELcSPQDELDFLMEALIISKFRHQNIVRCvgLSLRATPRLILL--ELM 593
Cdd:cd14103   1 LGRGKFGTVYR-----CVEKATGKELAAKFIKCR-KAKDREDVRNEIEIMNQLRHPRLLQL--YDAFETPREMVLvmEYV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 594 SGGDMksFLRHsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLlsCAGP-SRVAKIGDFGMARdiy 672
Cdd:cd14103  73 AGGEL--FERV----VDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENIL--CVSRtGNQIKIIDFGLAR--- 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 673 rasyyRRGDRALLPVKWMPPEaFL-------EGIfTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd14103 142 -----KYDPDKKLKVLFGTPE-FVapevvnyEPI-SYATDMWSVGVICYVLLS-GLSPFMGDNDAETLANVT 205
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
516-736 3.97e-09

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: 58.72  E-value: 3.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEglVIGLPGDSSPLQVAIKtlpelCSPQDELDFLMEALIISKFRHQNIVRcVGLSLRATPRLILL-ELMS 594
Cdd:cd14104   8 LGRGQFGIVHR--CVETSSKKTYMAKFVK-----VKGADQVLVKKEISILNIARHRNILR-LHESFESHEELVMIfEFIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNcLLSCAGPSRVAKIGDFGMAR----- 669
Cdd:cd14104  80 GVDIFERITTARFELNE------REIVSYVRQVCEALEFLHSKNIGHFDIRPEN-IIYCTRRGSYIKIIEFGQSRqlkpg 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 670 DIYRASYyrrgdralLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFV 736
Cdd:cd14104 153 DKFRLQY--------TSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPFEAETNQQTIENI 210
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
513-776 4.00e-09

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: 58.28  E-value: 4.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVyeglvIGLPGDSSPLQVAIKTLpELC--SPQDELDFLMEALIISKFRHQNIVRcVGLSLRATPRL-IL 589
Cdd:cd08218   5 IKKIGEGSFGKA-----LLVKSKEDGKQYVIKEI-NISkmSPKEREESRKEVAVLSKMKHPNIVQ-YQESFEENGNLyIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRPHLGqPSPLVMRDLLQLaqdiaqgCHYLEENH---FIHRDIAARNCLLSCAGpsrVAKIGDFG 666
Cdd:cd08218  78 MDYCDGGDLYKRINAQRGVLF-PEDQILDWFVQL-------CLALKHVHdrkILHRDIKSQNIFLTKDG---IIKLGDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MAR------DIYRA----SYYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFV 736
Cdd:cd08218 147 IARvlnstvELARTcigtPYY------------LSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKII 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42544153 737 VGGGRMDPPRGCPGpVYRIMTQCWQHEPELRPSFASILER 776
Cdd:cd08218 215 RGSYPPVPSRYSYD-LRSLVSQLFKRNPRDRPSINSILEK 253
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
512-724 4.13e-09

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: 58.85  E-value: 4.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYegLViglPGDSSPLQVAIKTLPELCSPQDElDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd14166   7 FMEVLGSGAFSEVY--LV---KQRSTGKLYALKCIKKSPLSRDS-SLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQdiaqgchYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMArdi 671
Cdd:cd14166  81 LVSGGELFDRILERGVYTEKDASRVINQVLSAVK-------YLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS--- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 672 yrasyyRRGDRALLPVK-----WMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14166 151 ------KMEQNGIMSTAcgtpgYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPF 201
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
514-767 4.81e-09

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 58.64  E-value: 4.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGLpgdssplQVAIKTLPELCspqdELDFLMEALIISK--FRHQNIVRCVGLSLRA----TPRL 587
Cdd:cd14144   1 RSVGKGRYGEVWKGKWRGE-------KVAVKIFFTTE----EASWFRETEIYQTvlMRHENILGFIAADIKGtgswTQLY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRphlgqpspLVMRDLLQLAQDIAQGCHYLEENHF--------IHRDIAARNCLL----SCAg 655
Cdd:cd14144  70 LITDYHENGSLYDFLRGNT--------LDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVkkngTCC- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 656 psrvakIGDFGMA-------RDIYRASYYRRGDRallpvKWMPPEAFLEGI----FTS--KTDSWSFGVLLWEI----FS 718
Cdd:cd14144 141 ------IADLGLAvkfisetNEVDLPPNTRVGTK-----RYMAPEVLDESLnrnhFDAykMADMYSFGLVLWEIarrcIS 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 719 LGY-----MPY----PGRTNQEVLDFVVGGGRMDPP-------RGCPGPVYRIMTQCWQHEPELR 767
Cdd:cd14144 210 GGIveeyqLPYydavPSDPSYEDMRRVVCVERRRPSipnrwssDEVLRTMSKLMSECWAHNPAAR 274
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
519-775 4.96e-09

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: 58.38  E-value: 4.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 519 GAFGEVYegLVI-GLPGDssplQVAIKTLPelcspQDELDF-------LMEALIISKFRHQNIVRCVgLSLRATPRL-IL 589
Cdd:cd05579   4 GAYGRVY--LAKkKSTGD----LYAIKVIK-----KRDMIRknqvdsvLAERNILSQAQNPFVVKLY-YSFQGKKNLyLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHsrphLGQPSPLVMRdlLQLAQdIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMAR 669
Cdd:cd05579  72 MEYLPGGDLYSLLEN----VGALDEDVAR--IYIAE-IVLALEYLHSHGIIHRDLKPDNILIDANG---HLKLTDFGLSK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 -DIYRASYYRRGDRALLPVK------------WMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPYPGRTNQEVLDFV 736
Cdd:cd05579 142 vGLVRRQIKLSIQKKSNGAPekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYE-FLVGIPPFHAETPEEIFQNI 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42544153 737 VgGGRMDPPRGC-PGPVYR-IMTQCWQHEPELRPSFASILE 775
Cdd:cd05579 221 L-NGKIEWPEDPeVSDEAKdLISKLLTPDPEKRLGAKGIEE 260
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
561-739 5.38e-09

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: 58.04  E-value: 5.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLlqlaqdiAQGCHYLEENHFI 640
Cdd:cd14185  48 EILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFDAIIESVKFTEHDAALMIIDL-------CEALVYIHSKHIV 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNCLLS-CAGPSRVAKIGDFGMARDIYRASYYRRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWeIFSL 719
Cdd:cd14185 121 HRDLKPENLLVQhNPDKSTTLKLADFGLAKYVTGPIFTVCGTPT-----YVAPEILSEKGYGLEVDMWAAGVILY-ILLC 194
                       170       180
                ....*....|....*....|..
gi 42544153 720 GYMPY--PGRTNQEVLDFVVGG 739
Cdd:cd14185 195 GFPPFrsPERDQEELFQIIQLG 216
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
561-724 5.50e-09

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: 58.14  E-value: 5.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVG-LSLRATPRLILL-ELMSGGDMksflrhsrphLGQPSPLVMRDllQLA----QDIAQGCHYL 634
Cdd:cd14118  64 EIAILKKLDHPNVVKLVEvLDDPNEDNLYMVfELVDKGAV----------MEVPTDNPLSE--ETArsyfRDIVLGIEYL 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 635 EENHFIHRDIAARNCLLSCAGpsRVaKIGDFGMARDIyrasyyrRGDRALL------PVkWMPPEAFLEG--IFTSK-TD 705
Cdd:cd14118 132 HYQKIIHRDIKPSNLLLGDDG--HV-KIADFGVSNEF-------EGDDALLsstagtPA-FMAPEALSESrkKFSGKaLD 200
                       170
                ....*....|....*....
gi 42544153 706 SWSFGVLLWeIFSLGYMPY 724
Cdd:cd14118 201 IWAMGVTLY-CFVFGRCPF 218
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
557-733 7.99e-09

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: 57.72  E-value: 7.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 557 DFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFlrhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEE 636
Cdd:cd14194  54 DIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDF-------LAEKESLTEEEATEFLKQILNGVYYLHS 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 637 NHFIHRDIAARNC-LLSCAGPSRVAKIGDFGMARDIYRASYYRrgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWE 715
Cdd:cd14194 127 LQIAHFDLKPENImLLDRNVPKPRIKIIDFGLAHKIDFGNEFK---NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYI 203
                       170
                ....*....|....*...
gi 42544153 716 IFSlGYMPYPGRTNQEVL 733
Cdd:cd14194 204 LLS-GASPFLGDTKQETL 220
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
522-724 8.47e-09

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: 57.74  E-value: 8.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 522 GEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFlMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSF 601
Cdd:cd06658  31 GEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLF-NEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 602 LRHSRPHLGQPSPLVMRDLLQLAqdiaqgchYLEENHFIHRDIAARNCLLSCAGpsRVaKIGDFGMARDIYRASYYRRGd 681
Cdd:cd06658 110 VTHTRMNEEQIATVCLSVLRALS--------YLHNQGVIHRDIKSDSILLTSDG--RI-KLSDFGFCAQVSKEVPKRKS- 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42544153 682 rALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd06658 178 -LVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPY 218
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
512-775 8.67e-09

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: 57.69  E-value: 8.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEglvIGLPGDSSplQVAIKTLpelcSPQDELDFLMEA---LIISKFRHQNIVRCVGLSLRATPRL- 587
Cdd:cd06639  26 IIETIGKGTYGKVYK---VTNKKDGS--LAAVKIL----DPISDVDEEIEAeynILRSLPNHPNVVKFYGMFYKADQYVg 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ----ILLELMSGGD----MKSFLRHSRpHLGQP--SPLVMRDLLqlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPs 657
Cdd:cd06639  97 gqlwLVLELCNGGSvtelVKGLLKCGQ-RLDEAmiSYILYGALL--------GLQHLHNNRIIHRDVKGNNILLTTEGG- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 rvAKIGDFGMARDIYRASyYRRGDRALLPVkWMPPEAF-----LEGIFTSKTDSWSFGVLLWE----------------I 716
Cdd:cd06639 167 --VKLVDFGVSAQLTSAR-LRRNTSVGTPF-WMAPEVIaceqqYDYSYDARCDVWSLGITAIEladgdpplfdmhpvkaL 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 717 FSLGYMPYPGRTNqevldfvvgggrmdPPRGCPGpVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd06639 243 FKIPRNPPPTLLN--------------PEKWCRG-FSHFISQCLIKDFEKRPSVTHLLE 286
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
512-724 8.70e-09

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: 57.49  E-value: 8.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL 589
Cdd:cd14076   5 LGRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKLIrrDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDM-KSFLRHSRphlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMA 668
Cdd:cd14076  85 LEFVSGGELfDYILARRR--------LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD---KNRNLVITDFGFA 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 669 RDIYRASYYRRGDRALLPVKWMPPEAFLEGIFT-SKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14076 154 NTFDHFNGDLMSTSCGSPCYAAPELVVSDSMYAgRKADIWSCGVILYAMLA-GYLPF 209
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
516-733 9.25e-09

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: 57.32  E-value: 9.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEgLViglpgDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14191  10 LGSGKFGQVFR-LV-----EKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMksFLRhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMARDIYRAs 675
Cdd:cd14191  84 GEL--FER----IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKI-KLIDFGLARRLENA- 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 yyrrGDRALL--PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14191 156 ----GSLKVLfgTPEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETL 210
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
516-724 1.25e-08

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: 56.95  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYegLVIGLPgdsSPLQVAIKTLPElcsPQDEL-DFLMEaLIISKF--RHQNIVRCVGLSLRATPRLILL-E 591
Cdd:cd13987   1 LGEGTYGKVL--LAVHKG---SGTKMALKFVPK---PSTKLkDFLRE-YNISLElsVHPHIIKTYDVAFETEDYYVFAqE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRhsrPHLGQPSPLVMRDLLQLAQDIAqgchYLEENHFIHRDIAARNCLL---SCagpsRVAKIGDFGMA 668
Cdd:cd13987  72 YAPYGDLFSIIP---PQVGLPEERVKRCAAQLASALD----FMHSKNLVHRDIKPENVLLfdkDC----RRVKLCDFGLT 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 669 RdiyrasyyRRGdrALLPVKW-----MPPE---AFLEGIFT--SKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd13987 141 R--------RVG--STVKRVSgtipyTAPEvceAKKNEGFVvdPSIDVWAFGVLLFCCLT-GNFPW 195
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
588-729 2.31e-08

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: 56.11  E-value: 2.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMksflrhsRPHLGQPSPlVMRDLLQL-AQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFG 666
Cdd:cd05578  77 MVVDLLLGGDL-------RYHLQQKVK-FSEETVKFyICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH---VHITDFN 145
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 667 MARDIYRASYY--RRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPYPGRTN 729
Cdd:cd05578 146 IATKLTDGTLAtsTSGTKP-----YMAPEVFMRAGYSFAVDWWSLGVTAYE-MLRGKRPYEIHSR 204
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
522-724 2.49e-08

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: 56.18  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 522 GEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFlMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSF 601
Cdd:cd06657  29 GEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLF-NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 602 LRHSRPHLGQPSPLVMRDLLQLAQDIAQGChyleenhfIHRDIAARNCLLSCAGpsRVaKIGDFGMARDIYRaSYYRRGD 681
Cdd:cd06657 108 VTHTRMNEEQIAAVCLAVLKALSVLHAQGV--------IHRDIKSDSILLTHDG--RV-KLSDFGFCAQVSK-EVPRRKS 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42544153 682 RALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd06657 176 LVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 216
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
516-737 2.50e-08

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: 56.07  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIglpgdSSPLQVAIKTL-PELCSPQDELDFLM-EALIISKFRHQNIVRCVGlSLRATPRL-ILLEL 592
Cdd:cd05581   9 LGEGSYSTVVLAKEK-----ETGKEYAIKVLdKRHIIKEKKVKYVTiEKEVLSRLAHPGIVKLYY-TFQDESKLyFVLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRHsrphLGQPSPLVMRdlLQLAQdIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMArDIY 672
Cdd:cd05581  83 APNGDLLEYIRK----YGSLDEKCTR--FYTAE-IVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGTA-KVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 673 RASYYRRGDRALLPVK----------------WMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFV 736
Cdd:cd05581 152 GPDSSPESTKGDADSQiaynqaraasfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRGSNEYLTFQKI 230

                .
gi 42544153 737 V 737
Cdd:cd05581 231 V 231
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
513-775 2.54e-08

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: 56.28  E-value: 2.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEglvigLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRH-QNIVRCVGLSLRATPRLILLE 591
Cdd:cd06617   6 IEELGRGAYGVVDK-----MRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDISMRSVDcPYTVTFYGALFREGDVWICME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGdMKSFLRHSRPH-LGQPSPLvmrdLLQLAQDIAQGCHYLEEN-HFIHRDIAARNCLLSCAGPsrvAKIGDFG--- 666
Cdd:cd06617  81 VMDTS-LDKFYKKVYDKgLTIPEDI----LGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ---VKLCDFGisg 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 -----MARDIyrasyyRRGDRALLPVKWMPPEAFLEGiFTSKTDSWSFGVLLWEIFSLGYmPYPG-RTNQEVLDFVVGGG 740
Cdd:cd06617 153 ylvdsVAKTI------DAGCKPYMAPERINPELNQKG-YDVKSDVWSLGITMIELATGRF-PYDSwKTPFQQLKQVVEEP 224
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42544153 741 RMDPPRGCPGPVYR-IMTQCWQHEPELRPSFASILE 775
Cdd:cd06617 225 SPQLPAEKFSPEFQdFVNKCLKKNYKERPNYPELLQ 260
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
604-669 2.70e-08

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: 56.52  E-value: 2.70e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 604 HSRPHLGQPSPLVMRDLL-QlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGPSR-VAKIGDFGMAR 669
Cdd:cd07842  97 HRQAKRVSIPPSMVKSLLwQ----ILNGIHYLHSNWVLHRDLKPANILVMGEGPERgVVKIGDLGLAR 160
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
552-743 3.30e-08

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: 56.18  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 552 PQDELDFLMEAliiskFRHQNIVRCVGLSLRATPRLILLELMSGGDM-KSFLRHSRphlgqpspLVMRDLLQLAQDIAQG 630
Cdd:cd14177  44 PSEEIEILMRY-----GQHPNIITLKDVYDDGRYVYLVTELMKGGELlDRILRQKF--------FSEREASAVLYTITKT 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 631 CHYLEENHFIHRDIAARNCL-LSCAGPSRVAKIGDFGMARDIyrasyyrRGDRALL-----PVKWMPPEAFLEGIFTSKT 704
Cdd:cd14177 111 VDYLHCQGVVHRDLKPSNILyMDDSANADSIRICDFGFAKQL-------RGENGLLltpcyTANFVAPEVLMRQGYDAAC 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42544153 705 DSWSFGVLLWEIFSlGYMPY---PGRTNQEVL------DFVVGGGRMD 743
Cdd:cd14177 184 DIWSLGVLLYTMLA-GYTPFangPNDTPEEILlrigsgKFSLSGGNWD 230
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
516-724 3.46e-08

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: 55.83  E-value: 3.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLviglpGDSSPLQVAIKTLPEL-CSPQDELDFLMEALIISKFRHQNIVRCVGlSLRATPR-----LIL 589
Cdd:cd14030  33 IGRGSFKTVYKGL-----DTETTVEVAWCELQDRkLSKSERQRFKEEAGMLKGLQHPNIVRFYD-SWESTVKgkkciVLV 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENH--FIHRDIAARNCLLScaGPSRVAKIGDFGM 667
Cdd:cd14030 107 TELMTSGTLKTYLKRFKV-------MKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFIT--GPTGSVKIGDLGL 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 668 ArDIYRASYYRrgdRALLPVKWMPPEAFLEGiFTSKTDSWSFGVLLWEIFSLGYmPY 724
Cdd:cd14030 178 A-TLKRASFAK---SVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEY-PY 228
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
519-775 4.06e-08

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 55.40  E-value: 4.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 519 GAFGEVYeglvigLPGDS-SPLQVAIKTLP-ELCSPQDeldflmeALIISKFRHQNIVRCVGLSLRATPRLILLELMSGG 596
Cdd:cd13995  15 GAFGKVY------LAQDTkTKKRMACKLIPvEQFKPSD-------VEIQACFRHENIAELYGALLWEETVHLFMEAGEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 597 DMKSFLRHSRPhlgqpsplvMR--DLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagpSRVAKIGDFGMARDIYRA 674
Cdd:cd13995  82 SVLEKLESCGP---------MRefEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM----STKAVLVDFGLSVQMTED 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 675 SYYRRGDRAllPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMP----YPgRTNQEVLDFVVggGRMDPP----- 745
Cdd:cd13995 149 VYVPKDLRG--TEIYMSPEVILCRGHNTKADIYSLGATIIHMQT-GSPPwvrrYP-RSAYPSYLYII--HKQAPPledia 222
                       250       260       270
                ....*....|....*....|....*....|
gi 42544153 746 RGCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd13995 223 QDCSPAMRELLEAALERNPNHRSSAAELLK 252
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
570-724 4.33e-08

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: 55.37  E-value: 4.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 570 HQNIVRCVGL---SLRATPRL-ILLELMSGGDMksFlrhSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIA 645
Cdd:cd14089  53 CPHIVRIIDVyenTYQGRKCLlVVMECMEGGEL--F---SRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 646 ARNCLLSCAGPSRVAKIGDFGMARDIYRAS---------YYrrgdrallpvkwMPPEAFLEGIFTSKTDSWSFGVLLWeI 716
Cdd:cd14089 128 PENLLYSSKGPNAILKLTDFGFAKETTTKKslqtpcytpYY------------VAPEVLGPEKYDKSCDMWSLGVIMY-I 194

                ....*...
gi 42544153 717 FSLGYMPY 724
Cdd:cd14089 195 LLCGYPPF 202
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
512-729 4.36e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 57.05  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   512 LLRALGHGAFGEVYegLVIGLPGDSSPLQVAI--KTLPElcspQDELDFLMEALIISKFRHQNIVRCVGLSL-RATPRL- 587
Cdd:PTZ00266   17 VIKKIGNGRFGEVF--LVKHKRTQEFFCWKAIsyRGLKE----REKSQLVIEVNVMRELKHKNIVRYIDRFLnKANQKLy 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   588 ILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLL-QLAQDIAQgCHYLEE----NHFIHRDIAARNCLLSCA-------- 654
Cdd:PTZ00266   91 ILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITrQLLHALAY-CHNLKDgpngERVLHRDLKPQNIFLSTGirhigkit 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153   655 ------GPSRVAKIGDFGMARDIYRASYYRRGdrALLPVKWmPPEAFLEGI--FTSKTDSWSFGVLLWEIFSlGYMPYPG 726
Cdd:PTZ00266  170 aqannlNGRPIAKIGDFGLSKNIGIESMAHSC--VGTPYYW-SPELLLHETksYDDKSDMWALGCIIYELCS-GKTPFHK 245

                  ...
gi 42544153   727 RTN 729
Cdd:PTZ00266  246 ANN 248
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
516-724 4.89e-08

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: 55.11  E-value: 4.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLViglpgDSSPLQVAIKTLPELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLILLELMS 594
Cdd:cd14082  11 LGSGQFGIVYGGKH-----RKTGRDVAIKVIDKLRFPTKQESQLRnEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 595 GGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRA 674
Cdd:cd14082  86 GDMLEMILSSEKGRLPE------RITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544153 675 SYYRR--GDRALLpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14082 160 SFRRSvvGTPAYL-----APEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPF 205
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
516-727 4.91e-08

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: 55.23  E-value: 4.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYeglviGLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVrCVGLSLRATPRLIL-LEL 592
Cdd:cd05577   1 LGRGGFGEVC-----ACQVKATGKMYACKKLDKkrIKKKKGETMALNEKIILEKVSSPFIV-SLAYAFETKDKLCLvLTL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMKSFLRhsrpHLGQPSpLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMARDIy 672
Cdd:cd05577  75 MNGGDLKYHIY----NVGTRG-FSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVR---ISDLGLAVEF- 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 673 raSYYRRGDRALLPVKWMPPEAFLEGI-FTSKTDSWSFGVLLWEIFSlGYMPYPGR 727
Cdd:cd05577 146 --KGGKKIKGRVGTHGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIA-GRSPFRQR 198
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
514-733 5.67e-08

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: 55.48  E-value: 5.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYegLVIGLPGDSSPLQVAIKTLPELC-SPQDELDFLMEALIISKFRHQNIVRcVGLSLRATPRLIL-LE 591
Cdd:cd05582   1 KVLGQGSFGKVF--LVRKITGPDAGTLYAMKVLKKATlKVRDRVRTKMERDILADVNHPFIVK-LHYAFQTEGKLYLiLD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMksFLRHSRPhlgqpsplVM---RDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMA 668
Cdd:cd05582  78 FLRGGDL--FTRLSKE--------VMfteEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGH---IKLTDFGLS 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 669 R---DIYRASYYRRGDrallpVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd05582 145 KesiDHEKKAYSFCGT-----VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETM 206
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
624-767 7.50e-08

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: 55.08  E-value: 7.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 624 AQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMAR-DIYRasyYRRGDRALLPVKWMPPEAFLEGIFTS 702
Cdd:cd05592 102 GAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH---IKIADFGMCKeNIYG---ENKASTFCGTPDYIAPEILKGQKYNQ 175
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 703 KTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVvgggRMDP---PRGCPGPVYRIMTQCWQHEPELR 767
Cdd:cd05592 176 SVDWWSFGVLLYEML-IGQSPFHGEDEDELFWSI----CNDTphyPRWLTKEAASCLSLLLERNPEKR 238
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
514-668 7.75e-08

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: 54.48  E-value: 7.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVR---------CVglslr 582
Cdd:cd14099   7 KFLGKGGFAKCYEVTDM-----STGKVYAGKVVPKssLTKPKQREKLKSEIKIHRSLKHPNIVKfhdcfedeeNV----- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 atprLILLELMSGGDMKSFLRHSRPhLGQPSplVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKI 662
Cdd:cd14099  77 ----YILLELCSNGSLMELLKRRKA-LTEPE--VRYFMRQ----ILSGVKYLHSNRIIHRDLKLGNLFLDENMN---VKI 142

                ....*.
gi 42544153 663 GDFGMA 668
Cdd:cd14099 143 GDFGLA 148
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
618-731 8.06e-08

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: 54.56  E-value: 8.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 618 RDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASYYRRgdrALLPVKWMPPEAFLE 697
Cdd:cd14197 111 KDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELRE---IMGTPEYVAPEILSY 187
                        90       100       110
                ....*....|....*....|....*....|....
gi 42544153 698 GIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQE 731
Cdd:cd14197 188 EPISTATDMWSIGVLAYVMLT-GISPFLGDDKQE 220
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
514-740 8.30e-08

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: 54.48  E-value: 8.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIglpgdSSPLQVAIKTL--PELCSPQDELdFLMEALIISKFRHQNIVRCVglSLRATPRLILL- 590
Cdd:cd14097   7 RKLGQGSFGVVIEATHK-----ETQTKWAIKKInrEKAGSSAVKL-LEREVDILKHVNHAHIIHLE--EVFETPKRMYLv 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 -ELMSGGDMKSFLRHSrphlGQPSPLVMRDLLQ-LAQDIAqgchYLEENHFIHRDIAARNCLLSCA----GPSRVAKIGD 664
Cdd:cd14097  79 mELCEDGELKELLLRK----GFFSENETRHIIQsLASAVA----YLHKNDIVHRDLKLENILVKSSiidnNDKLNIKVTD 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 665 FGMARDIYRASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPYPGRTNQEVLDFVVGGG 740
Cdd:cd14097 151 FGLSVQKYGLGEDMLQETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRKGD 224
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
561-724 9.00e-08

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: 54.08  E-value: 9.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMksFLRhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:cd14087  47 ELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGEL--FDR-----IIAKGSFTERDATRVLQMVLDGVKYLHGLGIT 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNCLLSCAGPSRVAKIGDFGMardiyrASYYRRGDRALLPV-----KWMPPEAFLEGIFTSKTDSWSFGVLLWE 715
Cdd:cd14087 120 HRDLKPENLLYYHPGPDSKIMITDFGL------ASTRKKGPNCLMKTtcgtpEYIAPEILLRKPYTQSVDMWAVGVIAYI 193

                ....*....
gi 42544153 716 IFSlGYMPY 724
Cdd:cd14087 194 LLS-GTMPF 201
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
516-733 9.27e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 55.43  E-value: 9.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  516 LGHGAFGEVYEGLVIglpgDSSPlQVAIKTLpeLCSPQDEldfLMEALIISKFRHQNIV--------RCVGLSLRATPRL 587
Cdd:PTZ00036  74 IGNGSFGVVYEAICI----DTSE-KVAIKKV--LQDPQYK---NRELLIMKNLNHINIIflkdyyytECFKKNEKNIFLN 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  588 ILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAqgchYLEENHFIHRDIAARNCLLScagP-SRVAKIGDFG 666
Cdd:PTZ00036 144 VVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALA----YIHSKFICHRDLKPQNLLID---PnTHTLKLCDFG 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153  667 MARDIY---RASYY--RRGDRAllpvkwmpPEAFLEGI-FTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVL 733
Cdd:PTZ00036 217 SAKNLLagqRSVSYicSRFYRA--------PELMLGATnYTTHIDLWSLGCIIAEMI-LGYPIFSGQSSVDQL 280
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
587-732 9.50e-08

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: 54.23  E-value: 9.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMksflrHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFG 666
Cdd:cd14172  77 LIIMECMEGGEL-----FSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFG 151
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASyyrrgdrALLPVKWMP----PEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPYPGRTNQEV 732
Cdd:cd14172 152 FAKETTVQN-------ALQTPCYTPyyvaPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPFYSNTGQAI 213
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
510-767 1.02e-07

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: 54.37  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGLPgdssplqVAIKTLpelcSPQDELDFLMEALIISK--FRHQNIVRCVGLSLRATPRL 587
Cdd:cd14142   7 ITLVECIGKGRYGEVWRGQWQGES-------VAVKIF----SSRDEKSWFRETEIYNTvlLRHENILGFIASDMTSRNSC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMS----GGDMKSFLRHSrphlgqpsPLVMRDLLQLAQDIAQGCHYLEENHF--------IHRDIAARNCL----L 651
Cdd:cd14142  76 TQLWLIThyheNGSLYDYLQRT--------TLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILvksnG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 SCAgpsrvakIGDFGMA-------RDIYRASYYRRGDRallpvKWMPPEAFLEGIFTS------KTDSWSFGVLLWEI-- 716
Cdd:cd14142 148 QCC-------IADLGLAvthsqetNQLDVGNNPRVGTK-----RYMAPEVLDETINTDcfesykRVDIYAFGLVLWEVar 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 717 --FSLG----YMP--YPGRTNQEVLD-----FVVGGGRMD-PPRGCPGPVY----RIMTQCWQHEPELR 767
Cdd:cd14142 216 rcVSGGiveeYKPpfYDVVPSDPSFEdmrkvVCVDQQRPNiPNRWSSDPTLtamaKLMKECWYQNPSAR 284
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
507-716 1.08e-07

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 54.24  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANV-TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPelCSPQDELDFLMEALIISKF-RHQNIVRCVGLSLRAT 584
Cdd:cd06636  14 PAGIfELVEVVGNGTYGQVYKGRHV-----KTGQLAAIKVMD--VTEDEEEEIKLEINMLKKYsHHRNIATYYGAFIKKS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PR------LILLELMSGGDMKSFLRHSRPHLGQPSPLVMrdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSR 658
Cdd:cd06636  87 PPghddqlWLVMEFCGAGSVTDLVKNTKGNALKEDWIAY-----ICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENA 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 659 VAKIGDFGMARDIYRaSYYRRGDRALLPVkWMPPEAFL-----EGIFTSKTDSWSFGVLLWEI 716
Cdd:cd06636 159 EVKLVDFGVSAQLDR-TVGRRNTFIGTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 219
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
550-777 1.10e-07

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 54.03  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 550 CSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLrhsrpHLGQPSPLVMRDLLQLAQDIAQ 629
Cdd:cd14057  31 VTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVL-----HEGTGVVVDQSQAVKFALDIAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 630 GC------------HYLEENH-FIHRDIAARncllscagpsrvakigdFGMArDIyRASYYRRGdRALLPVkWMPPEAFL 696
Cdd:cd14057 106 GMaflhtlepliprHHLNSKHvMIDEDMTAR-----------------INMA-DV-KFSFQEPG-KMYNPA-WMAPEALQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 697 ---EGIFTSKTDSWSFGVLLWEIFSLgYMPYPGRTNQEV-LDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSF-- 770
Cdd:cd14057 165 kkpEDINRRSADMWSFAILLWELVTR-EVPFADLSNMEIgMKIALEGLRVTIPPGISPHMCKLMKICMNEDPGKRPKFdm 243

                ....*...
gi 42544153 771 -ASILERL 777
Cdd:cd14057 244 iVPILEKM 251
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
513-739 1.15e-07

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: 54.02  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIgLPGDssplQVAIKTLP--ELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLIL- 589
Cdd:cd05611   1 LKPISKGAFGSVYLAKKR-STGD----YFAIKVLKksDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHsrphLGqpsPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMAr 669
Cdd:cd05611  76 MEYLNGGDCASLIKT----LG---GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH---LKLTDFGLS- 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 670 diyRASYYRRGDRALLPV-KWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPYPGRTNQEVLDFVVGG 739
Cdd:cd05611 145 ---RNGLEKRHNKKFVGTpDYLAPETILGVGDDKMSDWWSLGCVIFE-FLFGYPPFHAETPDAVFDNILSR 211
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
513-737 1.17e-07

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: 54.79  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLviglpgDS-SPLQVAIKTLpELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL---- 587
Cdd:cd07854  10 LRPLGCGSNGLVFSAV------DSdCDKRVAVKKI-VLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGSDLtedv 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ----------ILLELMSGgDMKSFLRHSrPHLGQPSPLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAgpS 657
Cdd:cd07854  83 gsltelnsvyIVQEYMET-DLANVLEQG-PLSEEHARLFMYQLLR-------GLKYIHSANVLHRDLKPANVFINTE--D 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 RVAKIGDFGMARdIYRASYYRRGDRAL-LPVKWM-PPEAFLE-GIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLD 734
Cdd:cd07854 152 LVLKIGDFGLAR-IVDPHYSHKGYLSEgLVTKWYrSPRLLLSpNNYTKAIDMWAAGCIFAEMLT-GKPLFAGAHELEQMQ 229

                ...
gi 42544153 735 FVV 737
Cdd:cd07854 230 LIL 232
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
507-716 1.34e-07

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: 54.34  E-value: 1.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANV-TLLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTLPELCSPQDELDflMEALIISKF-RHQNIVRCVGLSLRAT 584
Cdd:cd06637   4 PAGIfELVELVGNGTYGQVYKGRHV-----KTGQLAAIKVMDVTGDEEEEIK--QEINMLKKYsHHRNIATYYGAFIKKN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PR------LILLELMSGGDMKSFLRHSRphlgqPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSR 658
Cdd:cd06637  77 PPgmddqlWLVMEFCGAGSVTDLIKNTK-----GNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT---ENA 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 659 VAKIGDFGMARDIYRaSYYRRGDRALLPVkWMPPEAFL-----EGIFTSKTDSWSFGVLLWEI 716
Cdd:cd06637 149 EVKLVDFGVSAQLDR-TVGRRNTFIGTPY-WMAPEVIAcdenpDATYDFKSDLWSLGITAIEM 209
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
512-738 1.69e-07

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: 53.43  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLpelcspQDELDFLMEALI-------ISKFR---HQNIVRCVGLSL 581
Cdd:cd14133   3 VLEVLGKGTFGQVVKCY-----DLLTGEEVALKII------KNNKDYLDQSLDeirllelLNKKDkadKYHIVRLKDVFY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 582 RATPRLILLELMsGGDMKSFLRHSRPHlgqpsPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscAGPSRVA- 660
Cdd:cd14133  72 FKNHLCIVFELL-SQNLYEFLKQNKFQ-----YLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILL--ASYSRCQi 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 661 KIGDFGMARDIYRASYY---RRGDRAllpvkwmpPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVV 737
Cdd:cd14133 144 KIIDFGSSCFLTQRLYSyiqSRYYRA--------PEVILGLPYDEKIDMWSLGCILAELY-TGEPLFPGASEVDQLARII 214

                .
gi 42544153 738 G 738
Cdd:cd14133 215 G 215
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
624-767 1.70e-07

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: 54.16  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 624 AQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMAR-----DIYRASYYRRGDrallpvkWMPPEAFLEG 698
Cdd:cd05619 112 AAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH---IKIADFGMCKenmlgDAKTSTFCGTPD-------YIAPEILLGQ 181
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 699 IFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVvgggRMDP---PRGCPGPVYRIMTQCWQHEPELR 767
Cdd:cd05619 182 KYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSI----RMDNpfyPRWLEKEAKDILVKLFVREPERR 248
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
513-775 1.77e-07

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: 53.72  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIglpgdSSPLQVAIK--TLPELCSPQDELdfLMEALIISKFRHQNIVRCVGLSLRATPR---- 586
Cdd:cd14048  11 IQCLGRGGFGVVFEAKNK-----VDDCNYAVKriRLPNNELAREKV--LREVRALAKLDHPGIVRYFNAWLERPPEgwqe 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 -------LILLELMSGGDMKSFLR-----HSRPHLgqpsplVMrdlLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCA 654
Cdd:cd14048  84 kmdevylYIQMQLCRKENLKDWMNrrctmESRELF------VC---LNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 655 GpsrVAKIGDFGMAR---------------DIYRASYYRRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsl 719
Cdd:cd14048 155 D---VVKVGDFGLVTamdqgepeqtvltpmPAYAKHTGQVGTRL-----YMSPEQIHGNQYSEKVDIFALGLILFELI-- 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 720 gympYPGRTNQE-VLDFV-VGGGRMDPPRGCPGPVYRIMT-QCWQHEPELRPSFASILE 775
Cdd:cd14048 225 ----YSFSTQMErIRTLTdVRKLKFPALFTNKYPEERDMVqQMLSPSPSERPEAHEVIE 279
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
509-724 1.97e-07

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: 53.56  E-value: 1.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYegLVIGLPGDSsplQVAIKTLpelcSPQDELDF------LMEALIISKFRHQNIVRCVgLSLR 582
Cdd:cd14209   2 DFDRIKTLGTGSFGRVM--LVRHKETGN---YYAMKIL----DKQKVVKLkqvehtLNEKRILQAINFPFLVKLE-YSFK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLIL-LELMSGGDMKSFLRHSRpHLGQPSPLVMrdllqlAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAK 661
Cdd:cd14209  72 DNSNLYMvMEYVPGGEMFSHLRRIG-RFSEPHARFY------AAQIVLAFEYLHSLDLIYRDLKPENLLIDQQG---YIK 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 662 IGDFGMARDIyrasyyrRGDRALL---PvKWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPY 724
Cdd:cd14209 142 VTDFGFAKRV-------KGRTWTLcgtP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 198
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
509-768 2.05e-07

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: 53.28  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLviglPGDSSPLQVAIK----TLPELCSPQDELD-----FLMEALII-SKFRHQNIVRCVG 578
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVR----KKSNGQTLLALKeinmTNPAFGRTEQERDksvgdIISEVNIIkEQLRHPNIVRYYK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 579 LSLRATPRLILLELMSG---GDMKSFLRHSRPHLgqPSPLVMRDLLQLAQDIaqgcHYL-EENHFIHRDIAARNCLLsca 654
Cdd:cd08528  77 TFLENDRLYIVMELIEGaplGEHFSSLKEKNEHF--TEDRIWNIFVQMVLAL----RYLhKEKQIVHRDLKPNNIML--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 655 GPSRVAKIGDFGMARDIYRASYYRRGdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLgyMPYPGRTNQEVLD 734
Cdd:cd08528 148 GEDDKVTITDFGLAKQKGPESSKMTS--VVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTL--QPPFYSTNMLTLA 223
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42544153 735 FVVGGGRMDPprgCPGPVYR-----IMTQCWQHEPELRP 768
Cdd:cd08528 224 TKIVEAEYEP---LPEGMYSdditfVIRSCLTPDPEARP 259
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
511-731 2.23e-07

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: 53.09  E-value: 2.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVIGlpgDSSPLQVAIKTLPELCSPQDELDFLMEAL----IISKFRHQNIVRCVG-LSLRATP 585
Cdd:cd13990   3 LLLNLLGKGGFSEVYKAFDLV---EQRYVACKIHQLNKDWSEEKKQNYIKHALreyeIHKSLDHPRIVKLYDvFEIDTDS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLILLELMSGGDMKSFLRhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEE--NHFIHRDIAARNCLLSCAGPSRVAKIG 663
Cdd:cd13990  80 FCTVLEYCDGNDLDFYLK-------QHKSIPEREARSIIMQVVSALKYLNEikPPIIHYDLKPGNILLHSGNVSGEIKIT 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 664 DFGMARDIYRASYYRRG---DRALLPVKW-MPPEAFLEG----IFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQE 731
Cdd:cd13990 153 DFGLSKIMDDESYNSDGmelTSQGAGTYWyLPPECFVVGktppKISSKVDVWSVGVIFYQML-YGRKPFGHNQSQE 227
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
617-718 2.36e-07

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: 53.27  E-value: 2.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 617 MRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARdIYRASYYRRGDRALLPVKWMPPEAFL 696
Cdd:cd07864 122 MKQLLE-------GLNYCHKKNFLHRDIKCSNILLNNKGQ---IKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLL 190
                        90       100
                ....*....|....*....|...
gi 42544153 697 -EGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd07864 191 gEERYGPAIDVWSCGCILGELFT 213
PHA02988 PHA02988
hypothetical protein; Provisional
696-777 2.47e-07

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 53.21  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  696 LEGIF---TSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVGGGRMDP-PRGCPGPVYRIMTQCWQHEPELRPSFA 771
Cdd:PHA02988 192 LNDIFseyTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIINKNNSLKlPLDCPLEIKCIVEACTSHDSIKRPNIK 270

                 ....*.
gi 42544153  772 SILERL 777
Cdd:PHA02988 271 EILYNL 276
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
516-775 2.56e-07

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: 52.62  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVI--GLPgdssplqVAIKTLP--------ELCSPQD---ELDFLMEAliiSKFRHQNIVRCVGLSLR 582
Cdd:cd14005   8 LGKGGFGTVYSGVRIrdGLP-------VAVKFVPksrvtewaMINGPVPvplEIALLLKA---SKPGVPGVIRLLDWYER 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 583 ATPRLILLELMSGG-DMKSFLRHSRPHLGQPSPLVMRDLLQLAQDiaqgCHyleENHFIHRDIAARNCLLSCagPSRVAK 661
Cdd:cd14005  78 PDGFLLIMERPEPCqDLFDFITERGALSENLARIIFRQVVEAVRH----CH---QRGVLHRDIKDENLLINL--RTGEVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 662 IGDFGMArDIYRASYYR--RGDRAllpvkWMPPEAFLEGIFTSKT-DSWSFGVLLWEIFSlGYMPYpgRTNQEVLDFVVG 738
Cdd:cd14005 149 LIDFGCG-ALLKDSVYTdfDGTRV-----YSPPEWIRHGRYHGRPaTVWSLGILLYDMLC-GDIPF--ENDEQILRGNVL 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42544153 739 GgrmdpPRGCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14005 220 F-----RPRLSKECCDLISRCLQFDPSKRPSLEQILS 251
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
552-741 2.62e-07

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: 53.11  E-value: 2.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 552 PQDELDFLMEAliiskFRHQNIVRCVGLSLRATPRLILLELMSGGDM-KSFLRHSRphlgqpspLVMRDLLQLAQDIAQG 630
Cdd:cd14175  41 PSEEIEILLRY-----GQHPNIITLKDVYDDGKHVYLVTELMRGGELlDKILRQKF--------FSEREASSVLHTICKT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 631 CHYLEENHFIHRDIAARNCL-LSCAGPSRVAKIGDFGMARDIyrasyyrRGDRALL-----PVKWMPPEAFLEGIFTSKT 704
Cdd:cd14175 108 VEYLHSQGVVHRDLKPSNILyVDESGNPESLRICDFGFAKQL-------RAENGLLmtpcyTANFVAPEVLKRQGYDEGC 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42544153 705 DSWSFGVLLWEIFSlGYMPY---PGRTNQEVLDfVVGGGR 741
Cdd:cd14175 181 DIWSLGILLYTMLA-GYTPFangPSDTPEEILT-RIGSGK 218
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
511-731 3.06e-07

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 52.65  E-value: 3.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEglVIGLPGDSsplQVAIKTLPELcSPQDELDflMEALIISKF---RHqnIVRCVGLSLRATPRL 587
Cdd:cd14017   3 KVVKKIGGGGFGEIYK--VRDVVDGE---EVAMKVESKS-QPKQVLK--MEVAVLKKLqgkPH--FCRLIGCGRTERYNY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMsGGDMKSfLRHSRPhlgqPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGP-SRVAKIGDFG 666
Cdd:cd14017  73 IVMTLL-GPNLAE-LRRSQP----RGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSdERTVYILDFG 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 667 MAR-------DIYRASYYRRGDRalLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQE 731
Cdd:cd14017 147 LARqytnkdgEVERPPRNAAGFR--GTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFV-TGQLPWRKLKDKE 215
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
514-714 3.73e-07

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: 52.30  E-value: 3.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPELCSPQDELD-FLMEAL-IISKFRHQNIVRCVGLSLRATPRLIL-L 590
Cdd:cd14163   6 KTIGEGTYSKVKEAF-----SKKHQRKVAIKIIDKSGGPEEFIQrFLPRELqIVERLDHKNIIHVYEMLESADGKIYLvM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRPhlgQPSPLVMRDLLQLAQDIaQGCHYLeenHFIHRDIAARNCLLScagpSRVAKIGDFGMARD 670
Cdd:cd14163  81 ELAEDGDVFDCVLHGGP---LPEHRAKALFRQLVEAI-RYCHGC---GVAHRDLKCENALLQ----GFTLKLTDFGFAKQ 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42544153 671 IYRAsyYRRGDRALL-PVKWMPPEAfLEGI--FTSKTDSWSFGVLLW 714
Cdd:cd14163 150 LPKG--GRELSQTFCgSTAYAAPEV-LQGVphDSRKGDIWSMGVVLY 193
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
559-724 3.99e-07

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: 52.44  E-value: 3.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 559 LMEALIISKFRHQNIVRCVGLSLRATPRLIL-LELMSGGDMKSFLRHsrphLGQPSPLVmrdLLQLAQDIAQGCHYL-EE 636
Cdd:cd06620  51 LRELQILHECHSPYIVSFYGAFLNENNNIIIcMEYMDCGSLDKILKK----KGPFPEEV---LGKIAVAVLEGLTYLyNV 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 637 NHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDIYRA--------SYYrrgdrallpvkwMPPEAFLEGIFTSKTDSWS 708
Cdd:cd06620 124 HRIIHRDIKPSNILVNSKGQ---IKLCDFGVSGELINSiadtfvgtSTY------------MSPERIQGGKYSVKSDVWS 188
                       170
                ....*....|....*.
gi 42544153 709 FGVLLWEIfSLGYMPY 724
Cdd:cd06620 189 LGLSIIEL-ALGEFPF 203
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
509-734 4.08e-07

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: 52.22  E-value: 4.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEglvigLPGDSSPLQVAIKTLpELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14193   5 NVNKEEILGGGRFGQVHK-----CEEKSSGLKLAAKII-KARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMksFLRHsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMA 668
Cdd:cd14193  79 VMEYVDGGEL--FDRI----IDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQV-KIIDFGLA 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 669 RdiyrasyyRRGDRALLPVKWMPPEAFLEGI----FTS-KTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLD 734
Cdd:cd14193 152 R--------RYKPREKLRVNFGTPEFLAPEVvnyeFVSfPTDMWSLGVIAYMLLS-GLSPFLGEDDNETLN 213
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
513-724 4.28e-07

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: 52.60  E-value: 4.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEvyeglVIGLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd05607   7 FRVLGKGGFGE-----VCAVQVKNTGQMYACKKLDKkrLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRhsrpHLGQPSPLVMRDLLQLAQdIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAkigDFGMARD 670
Cdd:cd05607  82 SLMNGGDLKYHIY----NVGERGIEMERVIFYSAQ-ITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLS---DLGLAVE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 671 IY--RASYYRRGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd05607 154 VKegKPITQRAGTNG-----YMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF 203
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
561-745 4.42e-07

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 52.54  E-value: 4.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMkSFLRHSRPHLG-QPSPLV----MRDLLqlaqDIAQGCHyle 635
Cdd:cd14094  55 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADL-CFEIVKRADAGfVYSEAVashyMRQIL----EALRYCH--- 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 636 ENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASYYRRGdRALLPvKWMPPEAFLEGIFTSKTDSWSFGVLLWE 715
Cdd:cd14094 127 DNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGG-RVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFI 204
                       170       180       190
                ....*....|....*....|....*....|
gi 42544153 716 IFSlGYMPYPGRTNQEVLDFVVGGGRMDPP 745
Cdd:cd14094 205 LLS-GCLPFYGTKERLFEGIIKGKYKMNPR 233
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
589-745 5.28e-07

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: 52.64  E-value: 5.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMA 668
Cdd:cd05620  74 VMEFLNGGDLMF-------HIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH---IKIADFGMC 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RD-IY---RASYYrrgdrALLPvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVvgggRMDP 744
Cdd:cd05620 144 KEnVFgdnRASTF-----CGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESI----RVDT 212

                .
gi 42544153 745 P 745
Cdd:cd05620 213 P 213
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
570-727 5.57e-07

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: 52.03  E-value: 5.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 570 HQNIVRCVGLSLRATPRLILLELMSGGdmkSFLRH--SRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAAR 647
Cdd:cd14090  59 HPNILQLIEYFEDDERFYLVFEKMRGG---PLLSHieKRVHFTE------QEASLVVRDIASALDFLHDKGIAHRDLKPE 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 648 NCLlsCAGPSRVA--KIGDFGMARDIYRASYYRRGDRA---LLPV---KWMPPE---AFLEGIFT--SKTDSWSFGVLLW 714
Cdd:cd14090 130 NIL--CESMDKVSpvKICDFDLGSGIKLSSTSMTPVTTpelLTPVgsaEYMAPEvvdAFVGEALSydKRCDLWSLGVILY 207
                       170
                ....*....|...
gi 42544153 715 eIFSLGYMPYPGR 727
Cdd:cd14090 208 -IMLCGYPPFYGR 219
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
516-724 5.65e-07

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: 52.36  E-value: 5.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVyeglVIGLPGDSSPLqVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14168  18 LGTGAFSEV----VLAEERATGKL-FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMksFLRhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMAR-----D 670
Cdd:cd14168  93 GEL--FDR-----IVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKmegkgD 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42544153 671 IYRASYYRRGdrallpvkWMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14168 166 VMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 210
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
565-718 5.83e-07

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: 51.72  E-value: 5.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 565 ISKFRHQNIVR----------CVGLSLRATPRL------ILLELMSGGDMKSFLRHSRphlGQPSPLVMrdLLQLAQDIA 628
Cdd:cd14047  53 LAKLDHPNIVRyngcwdgfdyDPETSSSNSSRSktkclfIQMEFCEKGTLESWIEKRN---GEKLDKVL--ALEIFEQIT 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 629 QGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFG----MARDIYRASyyRRGDRallpvKWMPPEAFLEGIFTSKT 704
Cdd:cd14047 128 KGVEYIHSKKLIHRDLKPSNIFLVDTGK---VKIGDFGlvtsLKNDGKRTK--SKGTL-----SYMSPEQISSQDYGKEV 197
                       170
                ....*....|....
gi 42544153 705 DSWSFGVLLWEIFS 718
Cdd:cd14047 198 DIYALGLILFELLH 211
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
559-738 6.41e-07

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: 51.98  E-value: 6.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 559 LMEALIISKFRHQNIVRcvglslratprliLLELMSGGDMKS-FL-----RHSRPHL--GQPSPLVMRDLLQLAQDIAQG 630
Cdd:cd07845  54 LREITLLLNLRHPNIVE-------------LKEVVVGKHLDSiFLvmeycEQDLASLldNMPTPFSESQVKCLMLQLLRG 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 631 CHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARdiyrasyyrrgdRALLPVKWM----------PPEAFL-EGI 699
Cdd:cd07845 121 LQYLHENFIIHRDLKVSNLLLTDKG---CLKIADFGLAR------------TYGLPAKPMtpkvvtlwyrAPELLLgCTT 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42544153 700 FTSKTDSWSFGVLLWEIfsLGYMP-YPGRTNQEVLDFVVG 738
Cdd:cd07845 186 YTTAIDMWAVGCILAEL--LAHKPlLPGKSEIEQLDLIIQ 223
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
587-724 6.96e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 51.96  E-value: 6.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMksflrHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFG 666
Cdd:cd14170  75 LIVMECLDGGEL-----FSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFG 149
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 667 MARDIyrASYYRRGDRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14170 150 FAKET--TSHNSLTTPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPF 203
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
588-784 8.23e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 51.67  E-value: 8.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSR----PHLGQPSPLVMRDLLqlaqdiaqgchYLEENH-FIHRDIAARNCLLSCAGPSRVAKI 662
Cdd:cd06615  76 ICMEHMDGGSLDQVLKKAGripeNILGKISIAVLRGLT-----------YLREKHkIMHRDVKPSNILVNSRGEIKLCDF 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYrrGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEVL----DFVVG 738
Cdd:cd06615 145 GVSGQLIDSMANSFV--GTRS-----YMSPERLQGTHYTVQSDIWSLGLSLVEM-AIGRYPIPPPDAKELEamfgRPVSE 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 739 GGRMDPPRGCPGpvyrimtqcwqHEPELRPSFAsILERLQYCTQDP 784
Cdd:cd06615 217 GEAKESHRPVSG-----------HPPDSPRPMA-IFELLDYIVNEP 250
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
509-767 8.34e-07

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: 51.43  E-value: 8.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYEGLVIglpgDSSPLqVAIKTLPE---LCSPQDElDFLMEALIISKFRHQNIVRCVGlSLRATP 585
Cdd:cd05580   2 DFEFLKTLGTGSFGRVRLVKHK----DSGKY-YALKILKKakiIKLKQVE-HVLNEKRILSEVRHPFIVNLLG-SFQDDR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RL-ILLELMSGGDMKSFLRHSRpHLGQPSPLVMrdllqlAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGD 664
Cdd:cd05580  75 NLyMVMEYVPGGELFSLLRRSG-RFPNDVAKFY------AAEVVLALEYLHSLDIVYRDLKPENLLLDSDG---HIKITD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRASYYRRGDrallPvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY----PGRTNQEVLdfvvgGG 740
Cdd:cd05580 145 FGFAKRVKDRTYTLCGT----P-EYLAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFfdenPMKIYEKIL-----EG 213
                       250       260
                ....*....|....*....|....*..
gi 42544153 741 RMDPPRGCPGPVYRIMTQCWQHEPELR 767
Cdd:cd05580 214 KIRFPSFFDPDAKDLIKRLLVVDLTKR 240
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
561-724 9.61e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 51.27  E-value: 9.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMksFlrhsrphlgqpSPLVMRDLLQLA------QDIAQGCHYL 634
Cdd:cd14086  50 EARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGEL--F-----------EDIVAREFYSEAdashciQQILESVNHC 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 635 EENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASYYRRGdRALLPVkWMPPEAFLEGIFTSKTDSWSFGVLLW 714
Cdd:cd14086 117 HQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFG-FAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY 194
                       170
                ....*....|
gi 42544153 715 eIFSLGYMPY 724
Cdd:cd14086 195 -ILLVGYPPF 203
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
561-736 1.02e-06

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: 51.07  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRcvglsLRATPR-----LILLELMSGGDmksfLRHsrphlgqpsplVMRDLLQLAQDIAQ---GC- 631
Cdd:cd05572  43 EKEILEECNSPFIVK-----LYRTFKdkkylYMLMEYCLGGE----LWT-----------ILRDRGLFDEYTARfytACv 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 632 ----HYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDIYRasyyrrGDRAllpvkW--------MPPEAFLEGI 699
Cdd:cd05572 103 vlafEYLHSRGIIYRDLKPENLLLDSNG---YVKLVDFGFAKKLGS------GRKT-----WtfcgtpeyVAPEIILNKG 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42544153 700 FTSKTDSWSFGVLLWEIFSlGYMPY------PGRTNQEVLDFV 736
Cdd:cd05572 169 YDFSVDYWSLGILLYELLT-GRPPFggddedPMKIYNIILKGI 210
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
514-724 1.04e-06

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: 51.60  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYeglviGLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQN--IVRCVGLSLRATPRL-I 588
Cdd:cd05633  11 RIIGRGGFGEVY-----GCRKADTGKMYAMKCLDKkrIKMKQGETLALNERIMLSLVSTGDcpFIVCMTYAFHTPDKLcF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMA 668
Cdd:cd05633  86 ILDLMNGGDLHY-------HLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVR---ISDLGLA 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 669 RDIYRasyyRRGDRALLPVKWMPPEAFLEGI-FTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd05633 156 CDFSK----KKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPF 207
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
514-724 1.10e-06

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: 51.59  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYeglviGLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQN--IVRCVGLSLRATPRL-I 588
Cdd:cd14223   6 RIIGRGGFGEVY-----GCRKADTGKMYAMKCLDKkrIKMKQGETLALNERIMLSLVSTGDcpFIVCMSYAFHTPDKLsF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMA 668
Cdd:cd14223  81 ILDLMNGGDLHY-------HLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVR---ISDLGLA 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 669 RDIYRasyyRRGDRALLPVKWMPPEAFLEGI-FTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14223 151 CDFSK----KKPHASVGTHGYMAPEVLQKGVaYDSSADWFSLGCMLFKLLR-GHSPF 202
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
588-730 1.16e-06

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: 51.41  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGM 667
Cdd:cd14180  78 LVMELLRGGELLDRIKKKARFSESEASQLMRSLVS-------AVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGF 150
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 668 ARdiYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQ 730
Cdd:cd14180 151 AR--LRPQGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLS-GQVPFQSKRGK 210
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
627-744 1.27e-06

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: 50.59  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 627 IAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDiYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDS 706
Cdd:cd14111 108 ILQGLEYLHGRRVLHLDIKPDNIMVT---NLNAIKIVDFGSAQS-FNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADI 183
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 42544153 707 WSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVgGGRMDP 744
Cdd:cd14111 184 WSIGVLTYIMLS-GRSPFEDQDPQETEAKIL-VAKFDA 219
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
559-734 1.36e-06

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: 50.89  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 559 LMEALIISKFRHQNIVRCVGLsLRATPRLILLELMSGGDMKSFLRHSRphlGQPSPLVMRD-LLQLAQDIAQgCHyleEN 637
Cdd:cd07839  47 LREICLLKELKHKNIVRLYDV-LHSDKKLTLVFEYCDQDLKKYFDSCN---GDIDPEIVKSfMFQLLKGLAF-CH---SH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 638 HFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDI------YRAS----YYRrgdrallpvkwmPPEAFLEG-IFTSKTDS 706
Cdd:cd07839 119 NVLHRDLKPQNLLINKNGE---LKLADFGLARAFgipvrcYSAEvvtlWYR------------PPDVLFGAkLYSTSIDM 183
                       170       180
                ....*....|....*....|....*...
gi 42544153 707 WSFGVLLWEIFSLGYMPYPGRTNQEVLD 734
Cdd:cd07839 184 WSAGCIFAELANAGRPLFPGNDVDDQLK 211
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
514-774 1.54e-06

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: 50.70  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEglvigLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd14187  13 RFLGKGGFAKCYE-----ITDADTKEVFAGKIVPKslLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSggdMKSFLRHSRPHLGQPSPLVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDI 671
Cdd:cd14187  88 LCR---RRSLLELHKRRKALTEPEARYYLRQ----IILGCQYLHRNRVIHRDLKLGNLFLN---DDMEVKIGDFGLATKV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 yraSYYRRGDRALLPV-KWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLdFVVGGGRMDPPRGCPG 750
Cdd:cd14187 158 ---EYDGERKKTLCGTpNYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPFETSCLKETY-LRIKKNEYSIPKHINP 232
                       250       260
                ....*....|....*....|....
gi 42544153 751 PVYRIMTQCWQHEPELRPSFASIL 774
Cdd:cd14187 233 VAASLIQKMLQTDPTARPTINELL 256
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
630-737 1.56e-06

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: 51.15  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 630 GCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDiyrASYYrrGDRALL----PvKWMPPEAFLEGIFTSKTD 705
Cdd:cd05589 113 GLQFLHEHKIVYRDLKLDNLLLDTEG---YVKIADFGLCKE---GMGF--GDRTSTfcgtP-EFLAPEVLTDTSYTRAVD 183
                        90       100       110
                ....*....|....*....|....*....|..
gi 42544153 706 SWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVV 737
Cdd:cd05589 184 WWGLGVLIYEML-VGESPFPGDDEEEVFDSIV 214
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
514-727 1.73e-06

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: 50.79  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd05630   6 RVLGKGGFGEVCACQV-----RATGKMYACKKLEKkrIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHsrphLGQPSPLVMRDLLqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMARDI 671
Cdd:cd05630  81 LMNGGDLKFHIYH----MGQAGFPEARAVF-YAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIR---ISDLGLAVHV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 672 YRASYY--RRGDrallpVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGR 727
Cdd:cd05630 153 PEGQTIkgRVGT-----VGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFQQR 204
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
561-775 1.85e-06

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: 50.34  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQdiaqgchYLEENHFI 640
Cdd:cd14115  39 EAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQ-------YLHNCRVA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNCLLSCAGPSRVAKIGDFGmarDIYRASYYRRGDRALLPVKWMPPEaFLEGIFTS-KTDSWSFGVLLWEIFSl 719
Cdd:cd14115 112 HLDIKPENLLIDLRIPVPRVKLIDLE---DAVQISGHRHVHHLLGNPEFAAPE-VIQGTPVSlATDIWSIGVLTYVMLS- 186
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 720 GYMPYPGRTNQEVldfVVGGGRMD---PPR---GCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14115 187 GVSPFLDESKEET---CINVCRVDfsfPDEyfgDVSQAARDFINVILQEDPRRRPTAATCLQ 245
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
514-727 2.10e-06

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: 50.74  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd05632   8 RVLGKGGFGEVCACQV-----RATGKMYACKRLEKkrIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRHsrphLGQPSPLVMRDLLqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMARDI 671
Cdd:cd05632  83 IMNGGDLKFHIYN----MGNPGFEEERALF-YAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIR---ISDLGLAVKI 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 672 YRASYYRRgdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGR 727
Cdd:cd05632 155 PEGESIRG---RVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRGR 206
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
510-786 2.14e-06

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, 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 BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 50.43  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYEGLVIGLpgdssplQVAIKTLpelcSPQDELDFLMEALIISK--FRHQNIVRCVGLSLRATPRL 587
Cdd:cd14219   7 IQMVKQIGKGRYGEVWMGKWRGE-------KVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTGSW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMS----GGDMKSFLRhsrphlgqPSPLVMRDLLQLAQDIAQGCHYLEENHF--------IHRDIAARNCLLSCAG 655
Cdd:cd14219  76 TQLYLITdyheNGSLYDYLK--------STTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNILVKKNG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 656 PSRVAkigDFGMArdiyrASYYRRGDRALLPV-------KWMPPEAFLEGI----FTS--KTDSWSFGVLLWEI------ 716
Cdd:cd14219 148 TCCIA---DLGLA-----VKFISDTNEVDIPPntrvgtkRYMPPEVLDESLnrnhFQSyiMADMYSFGLILWEVarrcvs 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 717 ------FSLGYMPY-PGRTNQEVLDFVVGGGRMDPP-------RGCPGPVYRIMTQCWQHEPELRPSFASILERLQYCTQ 782
Cdd:cd14219 220 ggiveeYQLPYHDLvPSDPSYEDMREIVCIKRLRPSfpnrwssDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSE 299

                ....
gi 42544153 783 DPDV 786
Cdd:cd14219 300 SQDI 303
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
514-737 2.30e-06

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: 50.68  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgDSSPLQVAIKTLP-ELCSPQDELDFLM-EALIISKFRHQNIVRCVGLSLRATPRLI-LL 590
Cdd:cd05590   1 RVLGKGSFGKVMLARL-----KESGRLYAVKVLKkDVILQDDDVECTMtEKRILSLARNHPFLTQLYCCFQTPDRLFfVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHSRpHLGQPSPLVMrdllqlAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAkigDFGMARD 670
Cdd:cd05590  76 EFVNGGDLMFHIQKSR-RFDEARARFY------AAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLA---DFGMCKE 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544153 671 -----IYRASYYRRGDrallpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd05590 146 gifngKTTSTFCGTPD-------YIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFEAIL 209
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
588-784 2.42e-06

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: 50.44  E-value: 2.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFI-HRDIAARNCLLSCAGPSRVAKIGDFG 666
Cdd:cd06650  80 ICMEHMDGGSLDQVLK-------KAGRIPEQILGKVSIAVIKGLTYLREKHKImHRDVKPSNILVNSRGEIKLCDFGVSG 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 667 MARDIYRASYYrrGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQEvLDFVVGGGRMDPPR 746
Cdd:cd06650 153 QLIDSMANSFV--GTRS-----YMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYPIPPPDAKE-LELMFGCQVEGDAA 223
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42544153 747 GCPGPVYRIMTQCWQHEPELRPSFAsILERLQYCTQDP 784
Cdd:cd06650 224 ETPPRPRTPGRPLSSYGMDSRPPMA-IFELLDYIVNEP 260
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
509-724 2.50e-06

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: 50.00  E-value: 2.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYegLVIGLPGDSSPLQVAIKTLPElcspqdeldflmeALIISKFR---HQNIVRCVGLSLRATP 585
Cdd:cd05613   1 NFELLKVLGTGAYGKVF--LVRKVSGHDAGKLYAMKVLKK-------------ATIVQKAKtaeHTRTERQVLEHIRQSP 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLI--------------LLELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL 651
Cdd:cd05613  66 FLVtlhyafqtdtklhlILDYINGGELFT-------HLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 652 SCAGPsrvAKIGDFGMARDiYRASYYRRGDRALLPVKWMPPEAFLEGI--FTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd05613 139 DSSGH---VVLTDFGLSKE-FLLDENERAYSFCGTIEYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF 208
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
514-775 2.61e-06

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: 49.63  E-value: 2.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEglvigLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd14188   7 KVLGKGGFAKCYE-----MTDLTTNKVYAAKIIPHsrVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMSGGDMKSFLRhSRPHLGQPSplvMRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDI 671
Cdd:cd14188  82 YCSRRSMAHILK-ARKVLTEPE---VRYYLR---QIVSGLKYLHEQEILHRDLKLGNFFIN---ENMELKVGDFGLAARL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYYRRgdRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPgRTNQEVLDFVVGGGRMDPPRGCPGP 751
Cdd:cd14188 152 EPLEHRRR--TICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFE-TTNLKETYRCIREARYSLPSSLLAP 227
                       250       260
                ....*....|....*....|....
gi 42544153 752 VYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14188 228 AKHLIASMLSKNPEDRPSLDEIIR 251
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
588-727 2.75e-06

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: 50.05  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKsFLRHSrphLGQPSPLVMRDLLQLAQdIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGM 667
Cdd:cd05605  77 LVLTIMNGGDLK-FHIYN---MGNPGFEEERAVFYAAE-ITCGLEHLHSERIVYRDLKPENILLDDHGHVR---ISDLGL 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 668 ARDIyrasyyRRGDRA---LLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGR 727
Cdd:cd05605 149 AVEI------PEGETIrgrVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIE-GQAPFRAR 204
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
508-746 3.69e-06

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: 49.74  E-value: 3.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 508 ANVTLLRALGHGAFGEVYeglvigLPGDSSPLQ-VAIKTL--PELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRAT 584
Cdd:cd05612   1 DDFERIKTIGTGTFGRVH------LVRDRISEHyYALKVMaiPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 585 PRLILLELMSGGDMKSFLRHSRPHLGQPSplvmrdlLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGD 664
Cdd:cd05612  75 FLYMLMEYVPGGELFSYLRNSGRFSNSTG-------LFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH---IKLTD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRASYYRRGDrallpvkwmpPEAFLEGIFTSK-----TDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVVgG 739
Cdd:cd05612 145 FGFAKKLRDRTWTLCGT----------PEYLAPEVIQSKghnkaVDWWALGILIYEMLV-GYPPFFDDNPFGIYEKIL-A 212

                ....*..
gi 42544153 740 GRMDPPR 746
Cdd:cd05612 213 GKLEFPR 219
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
589-737 3.71e-06

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: 50.00  E-value: 3.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDM----KSFLRHSRPHLgqpsplvmrdlLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGD 664
Cdd:cd05616  79 VMEYVNGGDLmyhiQQVGRFKEPHA-----------VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH---IKIAD 144
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 665 FGMARD-----IYRASYYRRGDrallpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd05616 145 FGMCKEniwdgVTTKTFCGTPD-------YIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSIM 214
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
514-767 3.84e-06

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 49.65  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGLpgdssplQVAIKTLpelcSPQDELDFLMEALIISK--FRHQNIVRCVGLSLRATPRLILLE 591
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRGE-------KVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTGSWTQLY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 592 LMS----GGDMKSFLRHSrphlgqpsPLVMRDLLQLAQDIAQG-CHYLEENH-------FIHRDIAARNCLLSCAGPSRV 659
Cdd:cd14220  70 LITdyheNGSLYDFLKCT--------TLDTRALLKLAYSAACGlCHLHTEIYgtqgkpaIAHRDLKSKNILIKKNGTCCI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AkigDFGMArdiyrASYYRRGDRALLPV-------KWMPPEAFLEGIFTSK------TDSWSFGVLLWE---------IF 717
Cdd:cd14220 142 A---DLGLA-----VKFNSDTNEVDVPLntrvgtkRYMAPEVLDESLNKNHfqayimADIYSFGLIIWEmarrcvtggIV 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 718 SLGYMPY----PGRTNQEVLDFVVGGGRMDPPRG-------CPGPVYRIMTQCWQHEPELR 767
Cdd:cd14220 214 EEYQLPYydmvPSDPSYEDMREVVCVKRLRPTVSnrwnsdeCLRAVLKLMSECWAHNPASR 274
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
512-736 3.94e-06

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 50.09  E-value: 3.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPElcSPQDELDFLMEALIISKFRHQN-----IVRCVGLSLRATPR 586
Cdd:cd14228  19 VLEFLGRGTFGQVAKCW-----KRSTKEIVAIKILKN--HPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNHT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGgDMKSFLRHSRPhlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL--SCAGPSRVaKIGD 664
Cdd:cd14228  92 CLVFEMLEQ-NLYDFLKQNKF-----SPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdPVRQPYRV-KVID 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRA--------SYYRrgdrallpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFV 736
Cdd:cd14228 165 FGSASHVSKAvcstylqsRYYR------------APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGASEYDQIRYI 231
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
544-724 5.26e-06

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: 49.19  E-value: 5.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 544 KTLPELC-SPQDELD-FLMEALIISKFRHQNIVRCVG-LSLRATPRL-ILLELMSGGdmksflrhsrPHLGQPS--PLVM 617
Cdd:cd14199  56 RAAPEGCtQPRGPIErVYQEIAILKKLDHPNVVKLVEvLDDPSEDHLyMVFELVKQG----------PVMEVPTlkPLSE 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 618 RDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscaGPSRVAKIGDFGMARDIyrasyyrRGDRALL------PVkWMP 691
Cdd:cd14199 126 DQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV---GEDGHIKIADFGVSNEF-------EGSDALLtntvgtPA-FMA 194
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42544153 692 PEAFLE--GIFTSKT-DSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14199 195 PETLSEtrKIFSGKAlDVWAMGVTLY-CFVFGQCPF 229
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
588-784 5.47e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 49.28  E-value: 5.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGDMKSFLRHSR--PH--LGQPSPLVMRdllqlaqdiaqGCHYLEENHFI-HRDIAARNCLLSCAGPSRVAKI 662
Cdd:cd06649  80 ICMEHMDGGSLDQVLKEAKriPEeiLGKVSIAVLR-----------GLAYLREKHQImHRDVKPSNILVNSRGEIKLCDF 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 663 GDFGMARDIYRASYYrrGDRAllpvkWMPPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRTNQE--------VLD 734
Cdd:cd06649 149 GVSGQLIDSMANSFV--GTRS-----YMSPERLQGTHYSVQSDIWSMGLSLVEL-AIGRYPIPPPDAKEleaifgrpVVD 220
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 735 FVVGGGRMDPPRgcPGPVYRIMTqcwQHEPELRPSFAsILERLQYCTQDP 784
Cdd:cd06649 221 GEEGEPHSISPR--PRPPGRPVS---GHGMDSRPAMA-IFELLDYIVNEP 264
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
512-738 5.65e-06

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: 49.29  E-value: 5.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLviglpGDSSPLQVAIKTLPE-LCSPQDELDFLMEALIISKFRHQNIVrCVGLSLRATPRL--- 587
Cdd:cd07855   9 PIETIGSGAYGVVCSAI-----DTKSGQKVAIKKIPNaFDVVTTAKRTLRELKILRHFKHDNII-AIRDILRPKVPYadf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ----ILLELMSGgDMksflrHSRPHLGQPSPLvmrDLLQ--LAQdIAQGCHYLEENHFIHRDIAARNCLLS--CAgpsrv 659
Cdd:cd07855  83 kdvyVVLDLMES-DL-----HHIIHSDQPLTL---EHIRyfLYQ-LLRGLKYIHSANVIHRDLKPSNLLVNenCE----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFGMARDIYRAS----YYRRGDRALLPVKwmPPEAFLE-GIFTSKTDSWSFGVLLWEIfsLGYMP-YPGRTNQEVL 733
Cdd:cd07855 148 LKIGDFGMARGLCTSPeehkYFMTEYVATRWYR--APELMLSlPEYTQAIDMWSVGCIFAEM--LGRRQlFPGKNYVHQL 223

                ....*
gi 42544153 734 DFVVG 738
Cdd:cd07855 224 QLILT 228
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
513-775 5.95e-06

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: 48.90  E-value: 5.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVYEGLVIgLPGDssplQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd14046  11 LQVLGKGAFGQVVKVRNK-LDGR----YYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSggdmKSFLRHS-RPHLGQPSplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDI 671
Cdd:cd14046  86 CE----KSTLRDLiDSGLFQDT----DRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN---VKIGDFGLATSN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 672 YRASYYRRGD----------------RALLPVKWMPPEafLEGIFTS----KTDSWSFGVLLWEifslgyMPYPGRTNQE 731
Cdd:cd14046 155 KLNVELATQDinkstsaalgssgdltGNVGTALYVAPE--VQSGTKStyneKVDMYSLGIIFFE------MCYPFSTGME 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 732 ---VLDFVVGGGRMDPP--RGCPGPVYRIMTQC-WQHEPELRPSFASILE 775
Cdd:cd14046 227 rvqILTALRSVSIEFPPdfDDNKHSKQAKLIRWlLNHDPAKRPSAQELLK 276
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
512-733 6.06e-06

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: 49.08  E-value: 6.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLviglpgD-SSPLQVAIKTLpelcspQDELDFLMEAL----IISKFRH------QNIVR----- 575
Cdd:cd14210  17 VLSVLGKGSFGQVVKCL------DhKTGQLVAIKII------RNKKRFHQQALvevkILKHLNDndpddkHNIVRykdsf 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 576 ------CvglslratprlILLELMSGgDMKSFLRhSRPHLGQPSPLVMRdllqLAQDIAQGCHYLEENHFIHRDIAARNC 649
Cdd:cd14210  85 ifrghlC-----------IVFELLSI-NLYELLK-SNNFQGLSLSLIRK----FAKQILQALQFLHKLNIIHCDLKPENI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 650 LLSCAGPSRVaKIGDFGMA----RDIY-----RasYYRrgdrallpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFSlG 720
Cdd:cd14210 148 LLKQPSKSSI-KVIDFGSScfegEKVYtyiqsR--FYR------------APEVILGLPYDTAIDMWSLGCILAELYT-G 211
                       250
                ....*....|...
gi 42544153 721 YMPYPGRTNQEVL 733
Cdd:cd14210 212 YPLFPGENEEEQL 224
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
516-733 6.66e-06

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: 48.36  E-value: 6.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEglvigLPGDSSPLQVAIKTLPELCSPQDELdfLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd14108  10 IGRGAFSYLRR-----VKEKSSDLSFAAKFIPVRAKKKTSA--RRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRhsRPHLGQPS-PLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMARDIY-- 672
Cdd:cd14108  83 ELLERITK--RPTVCESEvRSYMRQLLE-------GIEYLHQNDVLHLDLKPENLLMADQKTDQV-RICDFGNAQELTpn 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 673 RASYYRRGdralLPvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14108 153 EPQYCKYG----TP-EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLT-GISPFVGENDRTTL 207
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
552-775 7.13e-06

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: 48.38  E-value: 7.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 552 PQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDmksfLRHSRPHLGQPSPLVMRDLLqlaQDIAQGC 631
Cdd:cd14110  40 PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPE----LLYNLAERNSYSEAEVTDYL---WQILSAV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 632 HYLEENHFIHRDIAARNCLLScaGPSRVaKIGDFGMARDiYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGV 711
Cdd:cd14110 113 DYLHSRRILHLDLRSENMIIT--EKNLL-KIVDLGNAQP-FNQGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGV 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 712 LLWEIFSLGYmPYPGRTNQEvLDFVVGGGRMDPPR---GCPGPVYRIMTQCWQHEPELRPSFASILE 775
Cdd:cd14110 189 TAFIMLSADY-PVSSDLNWE-RDRNIRKGKVQLSRcyaGLSGGAVNFLKSTLCAKPWGRPTASECLQ 253
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
612-717 7.22e-06

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: 48.66  E-value: 7.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 612 PSPLVMRDL-LQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVAKIGDFGMA-RDIY---RASYYRRGDRALL- 685
Cdd:cd14049 113 PYTPVDVDVtTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLH--GSDIHVRIGDFGLAcPDILqdgNDSTTMSRLNGLTh 190
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 42544153 686 -----PVKWMPPEAfLEGI-FTSKTDSWSFGVLLWEIF 717
Cdd:cd14049 191 tsgvgTCLYAAPEQ-LEGShYDFKSDMYSIGVILLELF 227
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
516-718 7.44e-06

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 48.78  E-value: 7.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFR-HQNIVRCVGL-----SLRATPRLIL 589
Cdd:cd14020   8 LGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESGDYGFAKERAALEQLQgHRNIVTLYGVftnhySANVPSRCLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSrphlgqPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScaGPSRVAKIGDFGMAr 669
Cdd:cd14020  88 LELLDVSVSELLLRSS------NQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWS--AEDECFKLIDFGLS- 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 670 diyrasyYRRGDRALLPVK---WMPPEAFL-----------EGIFTSKTDSWSFGVLLWEIFS 718
Cdd:cd14020 159 -------FKEGNQDVKYIQtdgYRAPEAELqnclaqaglqsETECTSAVDLWSLGIVLLEMFS 214
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
511-724 8.42e-06

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 47.99  E-value: 8.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYEGLVI--GLPGDSSPLQVAIKTLPELCSPQ---DELDFLMEAL-------IISKFRHQNIVrcvg 578
Cdd:cd14019   4 RIIEKIGEGTFSSVYKAEDKlhDLYDRNKGRLVALKHIYPTSSPSrilNELECLERLGgsnnvsgLITAFRNEDQV---- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 579 lslratprLILLELMSGGDMKSFLRH-SRPHLGqpspLVMRDLLQLAQDIaqgcHyleENHFIHRDIAARNCLLSCAgpS 657
Cdd:cd14019  80 --------VAVLPYIEHDDFRDFYRKmSLTDIR----IYLRNLFKALKHV----H---SFGIIHRDVKPGNFLYNRE--T 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 658 RVAKIGDFGMARDI-YRASyyRRGDRALLPvKWMPPEAFLE-GIFTSKTDSWSFGVLLWEIFSLGYMPY 724
Cdd:cd14019 139 GKGVLVDFGLAQREeDRPE--QRAPRAGTR-GFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGRFPFF 204
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
512-726 8.51e-06

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: 48.87  E-value: 8.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLPElcSPQDELDFLMEALIISKFRHQN-----IVRCVGLSLRATPR 586
Cdd:cd14229   4 VLDFLGRGTFGQVVKCWKRG-----TNEIVAVKILKN--HPSYARQGQIEVGILARLSNENadefnFVRAYECFQHRNHT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGgDMKSFLRHSRPhlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLL--SCAGPSRVaKIGD 664
Cdd:cd14229  77 CLVFEMLEQ-NLYDFLKQNKF-----SPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdPVRQPYRV-KVID 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRA--------SYYRrgdrallpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPG 726
Cdd:cd14229 150 FGSASHVSKTvcstylqsRYYR------------APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 206
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
620-768 8.98e-06

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: 48.47  E-value: 8.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 620 LLQlaqdIAQGCHYLEEN-HFIHRDIAARNCLLSCAGpsrVAKIGDFGMARDI----YRASYYRRGDRALLPVK-----W 689
Cdd:cd14011 120 LLQ----ISEALSFLHNDvKLVHGNICPESVVINSNG---EWKLAGFDFCISSeqatDQFPYFREYDPNLPPLAqpnlnY 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 690 MPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQ---EVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPEL 766
Cdd:cd14011 193 LAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLlsyKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEV 272

                ..
gi 42544153 767 RP 768
Cdd:cd14011 273 RP 274
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
512-736 9.06e-06

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 48.93  E-value: 9.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLPElcSPQDELDFLMEALIISKFRHQ-----NIVRCVGLSLRATPR 586
Cdd:cd14227  19 VLEFLGRGTFGQVVKCWKRG-----TNEIVAIKILKN--HPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNHT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGgDMKSFLRHSRPhlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLscAGPSRV---AKIG 663
Cdd:cd14227  92 CLVFEMLEQ-NLYDFLKQNKF-----SPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIML--VDPSRQpyrVKVI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARDIYRA--------SYYRrgdrallpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDF 735
Cdd:cd14227 164 DFGSASHVSKAvcstylqsRYYR------------APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGASEYDQIRY 230

                .
gi 42544153 736 V 736
Cdd:cd14227 231 I 231
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
516-666 1.10e-05

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: 45.90  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYegLVIGLPgdsSPLQVAIK-----TLPELCSPQDELDFLMEALIISKfrhqNIVRCVGLSLRATPRLILL 590
Cdd:cd13968   1 MGEGASAKVF--WAEGEC---TTIGVAVKigddvNNEEGEDLESEMDILRRLKGLEL----NIPKVLVTEDVDGPNILLM 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153 591 ELMSGGDMKSFLrhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFG 666
Cdd:cd13968  72 ELVKGGTLIAYT--------QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS---EDGNVKLIDFG 136
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
559-746 1.21e-05

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 48.28  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  559 LMEALIISKFRHQNIVRCVgLSLRATPRL-ILLELMSGGDMKSFLRHSRphlgqpsplvmrdllQLAQDIAQGCH----- 632
Cdd:PTZ00263  66 AQEKSILMELSHPFIVNMM-CSFQDENRVyFLLEFVVGGELFTHLRKAG---------------RFPNDVAKFYHaelvl 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  633 ---YLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMARDIYRASYYRRGDrallpvkwmpPEAFLEGIFTSK-----T 704
Cdd:PTZ00263 130 afeYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAKKVPDRTFTLCGT----------PEYLAPEVIQSKghgkaV 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 42544153  705 DSWSFGVLLWEiFSLGYMPY----PGRTNQEVLDfvvggGRMDPPR 746
Cdd:PTZ00263 197 DWWTMGVLLYE-FIAGYPPFfddtPFRIYEKILA-----GRLKFPN 236
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
561-716 1.24e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 48.45  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  561 EALIISKFRHQNIVRCVG-LSLRATPRLILLELMSggDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHF 639
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGtFTYNKFTCLILPRYKT--DLYCYLAAKRN-------IAICDILAIERSVLRAIQYLHENRI 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  640 IHRDIAARNCLLScaGPSRVAkIGDFGMA---RDIYRASYYRRGDrallPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEI 716
Cdd:PHA03212 204 IHRDIKAENIFIN--HPGDVC-LGDFGAAcfpVDINANKYYGWAG----TIATNAPELLARDPYGPAVDIWSAGIVLFEM 276
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
561-730 1.27e-05

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: 47.90  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMksFLRhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFI 640
Cdd:cd14085  48 EIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGEL--FDR-----IVEKGYYSERDAADAVKQILEAVAYLHENGIV 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 641 HRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRasyyrrgDRALLPVKWMP----PEAFLEGIFTSKTDSWSFGVLLWeI 716
Cdd:cd14085 121 HRDLKPENLLYATPAPDAPLKIADFGLSKIVDQ-------QVTMKTVCGTPgycaPEILRGCAYGPEVDMWSVGVITY-I 192
                       170
                ....*....|....*
gi 42544153 717 FSLGYMP-YPGRTNQ 730
Cdd:cd14085 193 LLCGFEPfYDERGDQ 207
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
514-727 1.29e-05

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: 48.07  E-value: 1.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLViglpgDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQNIVRcVGLSLRATPRLIL-L 590
Cdd:cd05631   6 RVLGKGGFGEVCACQV-----RATGKMYACKKLEKkrIKKRKGEAMALNEKRILEKVNSRFVVS-LAYAYETKDALCLvL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLRHsrphLGQPSPLVMRDLLqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMARD 670
Cdd:cd05631  80 TIMNGGDLKFHIYN----MGNPGFDEQRAIF-YAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIR---ISDLGLAVQ 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 671 IYRASYYRRgdrALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGR 727
Cdd:cd05631 152 IPEGETVRG---RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPFRKR 204
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
552-741 1.40e-05

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: 48.09  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 552 PQDELDFLMEAliiskFRHQNIVRCVGLSLRATPRLILLELMSGGDM-KSFLRHSRphlgqpspLVMRDLLQLAQDIAQG 630
Cdd:cd14176  59 PTEEIEILLRY-----GQHPNIITLKDVYDDGKYVYVVTELMKGGELlDKILRQKF--------FSEREASAVLFTITKT 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 631 CHYLEENHFIHRDIAARNCL-LSCAGPSRVAKIGDFGMARDIyrasyyrRGDRALL-----PVKWMPPEAFLEGIFTSKT 704
Cdd:cd14176 126 VEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQL-------RAENGLLmtpcyTANFVAPEVLERQGYDAAC 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42544153 705 DSWSFGVLLWEIFSlGYMPY---PGRTNQEVLDfVVGGGR 741
Cdd:cd14176 199 DIWSLGVLLYTMLT-GYTPFangPDDTPEEILA-RIGSGK 236
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
559-718 1.53e-05

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 47.83  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  559 LMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGgDMKSFL----RHSRPHlgqpsplVMRDLLQlaqdIAQGCHYL 634
Cdd:PTZ00024  68 LRELKIMNEIKHENIMGLVDVYVEGDFINLVMDIMAS-DLKKVVdrkiRLTESQ-------VKCILLQ----ILNGLNVL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  635 EENHFIHRDIAARNCLLSCAGpsrVAKIGDFGMAR----DIYRASYYRRGD---RALLPVK----WMPPEAFLEGI--FT 701
Cdd:PTZ00024 136 HKWYFMHRDLSPANIFINSKG---ICKIADFGLARrygyPPYSDTLSKDETmqrREEMTSKvvtlWYRAPELLMGAekYH 212
                        170
                 ....*....|....*..
gi 42544153  702 SKTDSWSFGVLLWEIFS 718
Cdd:PTZ00024 213 FAVDMWSVGCIFAELLT 229
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
512-726 1.58e-05

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: 47.83  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLPELCSPQDELDflMEALIISKFRHQ-----NIVRCVGLSLRATPR 586
Cdd:cd14211   3 VLEFLGRGTFGQVVKCWKRG-----TNEIVAIKILKNHPSYARQGQ--IEVSILSRLSQEnadefNFVRAYECFQHKNHT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGgDMKSFLRHSRPhlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAG--PSRVaKIGD 664
Cdd:cd14211  76 CLVFEMLEQ-NLYDFLKQNKF-----SPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqPYRV-KVID 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 665 FGMARDIYRA--------SYYRrgdrallpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPG 726
Cdd:cd14211 149 FGSASHVSKAvcstylqsRYYR------------APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 205
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
561-714 1.63e-05

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: 47.44  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSF-LRHS--RPHLGQpsplvmrdllQLAQDIAQGCHYLEEN 637
Cdd:cd14077  63 EAALSSLLNHPHICRLRDFLRTPNHYYMLFEYVDGGQLLDYiISHGklKEKQAR----------KFARQIASALDYLHRN 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 638 HFIHRDIAARNCLLScagPSRVAKIGDFGMArDIYR---------ASYYRRGDRALLPVKWMPPEaflegiftskTDSWS 708
Cdd:cd14077 133 SIVHRDLKIENILIS---KSGNIKIIDFGLS-NLYDprrllrtfcGSLYFAAPELLQAQPYTGPE----------VDVWS 198

                ....*.
gi 42544153 709 FGVLLW 714
Cdd:cd14077 199 FGVVLY 204
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
610-728 1.70e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 47.68  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 610 GQPSPLVMRDLLQLAQDIaqgcHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARDIYRASYYRRGDraLLPVKW 689
Cdd:cd07848  96 GVPPEKVRSYIYQLIKAI----HWCHKNDIVHRDIKPENLLIS---HNDVLKLCDFGFARNLSEGSNANYTE--YVATRW 166
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42544153 690 M-PPEAFLEGIFTSKTDSWSFGVLLWEIfSLGYMPYPGRT 728
Cdd:cd07848 167 YrSPELLLGAPYGKAVDMWSVGCILGEL-SDGQPLFPGES 205
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
520-792 1.84e-05

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: 47.67  E-value: 1.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 520 AFGEVYEGLVIGLPGDSSPLQ--VAIK-TLPELCSpQDELDFLMEALIISK-FRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd08216   5 EIGKCFKGGGVVHLAKHKPTNtlVAVKkINLESDS-KEDLKFLQQEILTSRqLQHPNILPYVTSFVVDNDLYVVTPLMAY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 GDMKSFLRHSRPHlGQPSpLVMRDLLQlaqDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFgmaRDIYraS 675
Cdd:cd08216  84 GSCRDLLKTHFPE-GLPE-LAIAFILR---DVLNALEYIHSKGYIHRSVKASHILIS---GDGKVVLSGL---RYAY--S 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 676 YYRRGDRA----LLPV------KWMPPEAF---LEGiFTSKTDSWSFGV-------------------LLWEIFSlGYMP 723
Cdd:cd08216 151 MVKHGKRQrvvhDFPKsseknlPWLSPEVLqqnLLG-YNEKSDIYSVGItacelangvvpfsdmpatqMLLEKVR-GTTP 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 724 -------YPgRTNQEVLDFVVGGGrMDPPRGCPGPVY----------RIMTQCWQHEPELRPSFASILER--LQYCTQDP 784
Cdd:cd08216 229 qlldcstYP-LEEDSMSQSEDSST-EHPNNRDTRDIPyqrtfseafhQFVELCLQRDPELRPSASQLLAHsfFKQCRRSN 306

                ....*...
gi 42544153 785 DVLNSLLP 792
Cdd:cd08216 307 TSLLDLLK 314
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
516-724 2.27e-05

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 46.98  E-value: 2.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYeglvigLPGDSSP-LQVAIKTLP--ELCSPQDELDflMEALIISKFRHQNIVRCVGLSLRATPRLILLEL 592
Cdd:cd14083  11 LGTGAFSEVV------LAEDKATgKLVAIKCIDkkALKGKEDSLE--NEIAVLRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 593 MSGGDMksFLRhsrphLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCagPSRVAKI--GDFGMARD 670
Cdd:cd14083  83 VTGGEL--FDR-----IVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYS--PDEDSKImiSDFGLSKM 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 671 IyrasyyrrgDRALLPVK-----WMPPEAFLEGIFTSKTDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14083 154 E---------DSGVMSTAcgtpgYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPF 202
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
570-714 2.74e-05

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: 46.64  E-value: 2.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 570 HQNIVRCVGLSLRATPRLILLELMSGGDMKSF-LRHSRphlGQPSPLVMRDLLQLAQDIAQgCHYLeenHFIHRDIAARN 648
Cdd:cd14074  61 HPNVVRLYEVIDTQTKLYLILELGDGGDMYDYiMKHEN---GLNEDLARKYFRQIVSAISY-CHKL---HVVHRDLKPEN 133
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 649 CLLScaGPSRVAKIGDFGMARDiyrasyYRRG---DRALLPVKWMPPEAFLEGIFTS-KTDSWSFGVLLW 714
Cdd:cd14074 134 VVFF--EKQGLVKLTDFGFSNK------FQPGeklETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILY 195
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
511-734 2.95e-05

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: 47.18  E-value: 2.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 511 TLLRALGHGAFGEVYeglvIGLPGDSSPLqVAIKTLPE--------LCSPQDELDFLmeALIISKFrhqnivrCVGL--S 580
Cdd:cd05610   7 VIVKPISRGAFGKVY----LGRKKNNSKL-YAVKVVKKadminknmVHQVQAERDAL--ALSKSPF-------IVHLyyS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 581 LRATPRLIL-LELMSGGDMKSFLrHSRPHLGQPSPLVMRDLLQLAQDiaqgchYLEENHFIHRDIAARNCLLSCAGPsrv 659
Cdd:cd05610  73 LQSANNVYLvMEYLIGGDVKSLL-HIYGYFDEEMAVKYISEVALALD------YLHRHGIIHRDLKPDNMLISNEGH--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 660 AKIGDFG-----MARDI---------------------------------------YRA-SYYRRG------DRALLPVK 688
Cdd:cd05610 143 IKLTDFGlskvtLNRELnmmdilttpsmakpkndysrtpgqvlslisslgfntptpYRTpKSVRRGaarvegERILGTPD 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42544153 689 WMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPYPGRTNQEVLD 734
Cdd:cd05610 223 YLAPELLLGKPHGPAVDWWALGVCLFE-FLTGIPPFNDETPQQVFQ 267
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
512-743 2.98e-05

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: 46.86  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpgdSSPLQVAIKTL-PELCSPQDELDFLMEAliiskFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd14091   4 IKEEIGKGSYSVCKRCIHK-----ATGKEYAVKIIdKSKRDPSEEIEILLRY-----GQHPNIITLRDVYDDGNSVYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDM-KSFLRHsrPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAG--PSRVaKIGDFGM 667
Cdd:cd14091  74 ELLRGGELlDRILRQ--KFFSE------REASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESgdPESL-RICDFGF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 668 ARDIyrasyyrRGDRALL--P---VKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY---PGRTNQEVLDfVVGG 739
Cdd:cd14091 145 AKQL-------RAENGLLmtPcytANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFasgPNDTPEVILA-RIGS 215

                ....
gi 42544153 740 GRMD 743
Cdd:cd14091 216 GKID 219
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
570-727 2.98e-05

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: 46.96  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 570 HQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQlaqdiaqGCHYLEENHFIHRDIAARNC 649
Cdd:cd14179  61 HPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVS-------AVSHMHDVGVVHRDLKPENL 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 650 LLSCAGPSRVAKIGDFGMARdiyrasyYRRGDRALLP-----VKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14179 134 LFTDESDNSEIKIIDFGFAR-------LKPPDNQPLKtpcftLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPF 205

                ...
gi 42544153 725 PGR 727
Cdd:cd14179 206 QCH 208
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
512-724 3.08e-05

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: 46.48  E-value: 3.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGL--VIGLpgdssplQVAIKTLP--ELCSPQDELDFLMEALIISKFRHQNIVRCVGLsLRATPRL 587
Cdd:cd14081   5 LGKTLGKGQTGLVKLAKhcVTGQ-------KVAIKIVNkeKLSKESVLMKVEREIAIMKLIEHPNVLKLYDV-YENKKYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 IL-LELMSGGDMKSFLRHSRPhlgqpspLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFG 666
Cdd:cd14081  77 YLvLEYVSGGELFDYLVKKGR-------LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLD---EKNNIKIADFG 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544153 667 MARdiyrasyyrrgdrallpvkWMPPEAFLEgifTS--------------------KTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd14081 147 MAS-------------------LQPEGSLLE---TScgsphyacpevikgekydgrKADIWSCGVILYALLV-GALPF 201
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
588-726 3.25e-05

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: 46.56  E-value: 3.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 ILLELMSGGdmkSFLRH--SRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLlsCAGPSRVA--KIG 663
Cdd:cd14174  77 LVFEKLRGG---SILAHiqKRKHFNE------REASRVVRDIASALDFLHTKGIAHRDLKPENIL--CESPDKVSpvKIC 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 664 DFGMARDIyrasyyrRGDRALLPV------------KWMPP---EAFLE--GIFTSKTDSWSFGVLLWEIFSlGYMPYPG 726
Cdd:cd14174 146 DFDLGSGV-------KLNSACTPIttpelttpcgsaEYMAPevvEVFTDeaTFYDKRCDLWSLGVILYIMLS-GYPPFVG 217
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
561-718 3.48e-05

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 46.99  E-value: 3.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLI-LLELMSGGDMKSFLRHSRPHLGQPSPLVM-RDLLQ-LAQDIAQGCHYLEEN 637
Cdd:cd07867  49 EIALLRELKHPNVIALQKVFLSHSDRKVwLLFDYAEHDLWHIIKFHRASKANKKPMQLpRSMVKsLLYQILDGIHYLHAN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 638 HFIHRDIAARNCLLSCAGPSR-VAKIGDFGMARdIYRASYYRRGDraLLPVK---WMPPEAFLEGI--FTSKTDSWSFGV 711
Cdd:cd07867 129 WVLHRDLKPANILVMGEGPERgRVKIADMGFAR-LFNSPLKPLAD--LDPVVvtfWYRAPELLLGArhYTKAIDIWAIGC 205

                ....*..
gi 42544153 712 LLWEIFS 718
Cdd:cd07867 206 IFAELLT 212
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
541-669 4.43e-05

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 47.10  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  541 VAIKTL-PELCSPQDELD-FLMEALIISKFRHQNIVRC--VGlslrATPRL--ILLELMSGGDMKSFLRhsrphlgQPSP 614
Cdd:NF033483  35 VAVKVLrPDLARDPEFVArFRREAQSAASLSHPNIVSVydVG----EDGGIpyIVMEYVDGRTLKDYIR-------EHGP 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153  615 LVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMAR 669
Cdd:NF033483 104 LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIAR 155
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
509-745 5.58e-05

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: 46.07  E-value: 5.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 509 NVTLLRALGHGAFGEVYegLVIGLPGDSSPLQVAIKTLpelcspqdeldflMEALIISKFR---HQNIVRCVGLSLRATP 585
Cdd:cd05614   1 NFELLKVLGTGAYGKVF--LVRKVSGHDANKLYAMKVL-------------RKAALVQKAKtveHTRTERNVLEHVRQSP 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 586 RLI--------------LLELMSGGDMKSFLrHSRPHLGQPSPLVMRDLLQLAQDiaqgchYLEENHFIHRDIAARNCLL 651
Cdd:cd05614  66 FLVtlhyafqtdaklhlILDYVSGGELFTHL-YQRDHFSEDEVRFYSGEIILALE------HLHKLGIVYRDIKLENILL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 652 SCAGPsrvAKIGDFGMARDiYRASYYRRGDRALLPVKWMPPEaflegIFTSKT------DSWSFGVLLWEIFSlGYMPYP 725
Cdd:cd05614 139 DSEGH---VVLTDFGLSKE-FLTEEKERTYSFCGTIEYMAPE-----IIRGKSghgkavDWWSLGILMFELLT-GASPFT 208
                       250       260
                ....*....|....*....|....
gi 42544153 726 ----GRTNQEVLDFVVgggRMDPP 745
Cdd:cd05614 209 legeKNTQSEVSRRIL---KCDPP 229
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
502-737 6.04e-05

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: 46.14  E-value: 6.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 502 VTEVSPANVTLLRALGHGAFGEVYEGLVIGlpgdsSPLQVAIKTLPELCSPQDElDF---LMEALIISKFRHQNIVRCVG 578
Cdd:cd05615   4 LDRVRLTDFNFLMVLGKGSFGKVMLAERKG-----SDELYAIKILKKDVVIQDD-DVectMVEKRVLALQDKPPFLTQLH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 579 LSLRATPRL-ILLELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPs 657
Cdd:cd05615  78 SCFQTVDRLyFVMEYVNGGDLMY-------HIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 rvAKIGDFGMARDIYRASYYRRgDRALLPvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd05615 150 --IKIADFGMCKEHMVEGVTTR-TFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIM 224
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
509-737 6.20e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 46.13  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  509 NVTLLRALGHGAFGEVYegLVIGLPGDSSPlqVAIKTLpELCS--PQDELDFLM-EALIISKFRHQNIVRCVGLSLRATP 585
Cdd:PTZ00426  31 DFNFIRTLGTGSFGRVI--LATYKNEDFPP--VAIKRF-EKSKiiKQKQVDHVFsERKILNYINHPFCVNLYGSFKDESY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153  586 RLILLELMSGGDMKSFLRHSRPHLGQPSPLvmrdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGpsrVAKIGDF 665
Cdd:PTZ00426 106 LYLVLEFVIGGEFFTFLRRNKRFPNDVGCF-------YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDG---FIKMTDF 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544153  666 GMARDIYRASYYRRGDRallpvKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPY----PGRTNQEVLDFVV 737
Cdd:PTZ00426 176 GFAKVVDTRTYTLCGTP-----EYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCPPFyanePLLIYQKILEGII 245
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
561-718 7.42e-05

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 45.82  E-value: 7.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 561 EALIISKFRHQNIVRCVGLSLRATPRLI-LLELMSGGDMKSFLRHSRPHLGQPSPLVM-RDLLQ-LAQDIAQGCHYLEEN 637
Cdd:cd07868  64 EIALLRELKHPNVISLQKVFLSHADRKVwLLFDYAEHDLWHIIKFHRASKANKKPVQLpRGMVKsLLYQILDGIHYLHAN 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 638 HFIHRDIAARNCLLSCAGPSR-VAKIGDFGMARdIYRASYYRRGDraLLPVK---WMPPEAFLEGI--FTSKTDSWSFGV 711
Cdd:cd07868 144 WVLHRDLKPANILVMGEGPERgRVKIADMGFAR-LFNSPLKPLAD--LDPVVvtfWYRAPELLLGArhYTKAIDIWAIGC 220

                ....*..
gi 42544153 712 LLWEIFS 718
Cdd:cd07868 221 IFAELLT 227
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
513-737 8.71e-05

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: 45.84  E-value: 8.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 513 LRALGHGAFGEVyeglvIGLPGDSSPLQVAIKTLP-ELCSPQDELDF-LMEALIISKFRHQnIVRCVGLSLRATPRL-IL 589
Cdd:cd05593  20 LKLLGKGTFGKV-----ILVREKASGKYYAMKILKkEVIIAKDEVAHtLTESRVLKNTRHP-FLTSLKYSFQTKDRLcFV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 590 LELMSGGDMKSFLRHSRphlgqpspLVMRDLLQL-AQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDFGMA 668
Cdd:cd05593  94 MEYVNGGELFFHLSRER--------VFSEDRTRFyGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH---IKITDFGLC 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 669 RDIYRasyyrrgDRALLPV-----KWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV 737
Cdd:cd05593 163 KEGIT-------DAATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL 228
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
514-718 1.12e-04

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: 45.51  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEglvIGLPGDSSplQVAIKTLP----ELCSPQDeldFLMEALIISKFRHQNIVRcvGLSLRATPRL-- 587
Cdd:cd07853   6 RPIGYGAFGVVWS---VTDPRDGK--RVALKKMPnvfqNLVSCKR---VFRELKMLCFFKHDNVLS--ALDILQPPHIdp 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 588 -----ILLELMsggdmksflrHSRPH--LGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS--Cagpsr 658
Cdd:cd07853  76 feeiyVVTELM----------QSDLHkiIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNsnC----- 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 659 VAKIGDFGMAR----DIYR-------ASYYRrgdrallpvkwmPPEaFLEGI--FTSKTDSWSFGVLLWEIFS 718
Cdd:cd07853 141 VLKICDFGLARveepDESKhmtqevvTQYYR------------APE-ILMGSrhYTSAVDIWSVGCIFAELLG 200
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
519-775 1.36e-04

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: 44.72  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 519 GAFGEVYEGLVIGLPGDSSPLQVAIKTLPElcSPQDELDFLM---EALIISKFRHQNIVRCVGLSLRATPRLILLELMSG 595
Cdd:cd07846   7 GLVGEGSYGMVMKCRHKETGQIVAIKKFLE--SEDDKMVKKIamrEIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 596 ---GDMKSFlrhsrPHlGQPSPLVMRDLLQlaqdIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMAR--- 669
Cdd:cd07846  85 tvlDDLEKY-----PN-GLDESRVRKYLFQ----ILRGIDFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARtla 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 670 ---DIYRASYYRRGDRAllpvkwmpPEAFLEGIFTSK-TDSWSFGVLLWEIFSlGYMPYPGRTNQEVLDFVV-------- 737
Cdd:cd07846 152 apgEVYTDYVATRWYRA--------PELLVGDTKYGKaVDVWAVGCLVTEMLT-GEPLFPGDSDIDQLYHIIkclgnlip 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 738 -----------GGGRMDPPRGCPGPVYR-----------IMTQCWQHEPELRPSFASILE 775
Cdd:cd07846 223 rhqelfqknplFAGVRLPEVKEVEPLERrypklsgvvidLAKKCLHIDPDKRPSCSELLH 282
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
512-724 1.49e-04

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: 44.59  E-value: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGevyeglVIGLPGDSSPLQ-VAIKTLPElcspQDELDFLMEALIIS--KFRHQNIVRCVGLSLRATPRLI 588
Cdd:cd14665   4 LVKDIGSGNFG------VARLMRDKQTKElVAVKYIER----GEKIDENVQREIINhrSLRHPNIVRFKEVILTPTHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLRHSrphlGQPSPLVMRDLLqlaQDIAQGCHYLEENHFIHRDIAARNCLLScAGPSRVAKIGDFGMA 668
Cdd:cd14665  74 VMEYAAGGELFERICNA----GRFSEDEARFFF---QQLISGVSYCHSMQICHRDLKLENTLLD-GSPAPRLKICDFGYS 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 669 RDiyrASYYRRGDRALLPVKWMPPEAFLEGIFTSK-TDSWSFGVLLWeIFSLGYMPY 724
Cdd:cd14665 146 KS---SVLHSQPKSTVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLY-VMLVGAYPF 198
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
507-737 1.62e-04

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: 44.62  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 507 PANVTLLRALGHGAFGEVyegLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPR 586
Cdd:cd05602   6 PSDFHFLKVIGKGSFGKV---LLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 L-ILLELMSGGDMKSFLRHSRPHLgQPSPLVMrdllqlAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPsrvAKIGDF 665
Cdd:cd05602  83 LyFVLDYINGGELFYHLQRERCFL-EPRARFY------AAEIASALGYLHSLNIVYRDLKPENILLDSQGH---IVLTDF 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544153 666 GMARDiyraSYYRRGDRALL--PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQEVLDFVV 737
Cdd:cd05602 153 GLCKE----NIEPNGTTSTFcgTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMYDNIL 221
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
512-731 1.82e-04

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: 44.28  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpGDSSPLQVAIKTLPELCSPQDELDFLMEAL----IISKFRHQNIVRCVG-LSLRATPR 586
Cdd:cd14040  10 LLHLLGRGGFSEVYKAFDL---YEQRYAAVKIHQLNKSWRDEKKENYHKHACreyrIHKELDHPRIVKLYDyFSLDTDTF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENH--FIHRDIAARNCLLSCAGPSRVAKIGD 664
Cdd:cd14040  87 CTVLEYCEGNDLDFYLK-------QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITD 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 665 FGMARDIYRASYYRRG----DRALLPVKWMPPEAFLEG----IFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQE 731
Cdd:cd14040 160 FGLSKIMDDDSYGVDGmdltSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQ 233
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
564-712 2.09e-04

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: 44.11  E-value: 2.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 564 IISKFRHQNIVRCVG-LSLRATPRLILlELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHR 642
Cdd:cd14107  51 ILARLSHRRLTCLLDqFETRKTLILIL-ELCSSEELLD-------RLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHL 122
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544153 643 DIAARNCLLscAGPSRV-AKIGDFGMARDI--YRASYYRRGDRallpvKWMPPEAFLEGIFTSKTDSWSFGVL 712
Cdd:cd14107 123 DIKPDNILM--VSPTREdIKICDFGFAQEItpSEHQFSKYGSP-----EFVAPEIVHQEPVSAATDIWALGVI 188
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
514-769 2.14e-04

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: 44.04  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIgLPGDssplQVAIKTLPELCSPQDEL---DFLMEALIISKFRHQNIVRCVGLSLRATPRLILL 590
Cdd:cd14070   8 RKLGEGSFAKVREGLHA-VTGE----KVAIKVIDKKKAKKDSYvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScagPSRVAKIGDFGMARD 670
Cdd:cd14070  83 ELCPGGNLMH-------RIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLD---ENDNIKLIDFGLSNC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 671 IYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYP------GRTNQEVLDfvvggGRMDP 744
Cdd:cd14070 153 AGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTvepfslRALHQKMVD-----KEMNP 226
                       250       260
                ....*....|....*....|....*.
gi 42544153 745 -PRGCPGPVYRIMTQCWQHEPELRPS 769
Cdd:cd14070 227 lPTDLSPGAISFLRSLLEPDPLKRPN 252
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
516-671 2.95e-04

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 43.88  E-value: 2.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYEGLVIGLPGDSSPlqVAIKtlpeLCSPQDELDF-----LMEALIISKFRHqNIVRCVGLSLRATPRLILL 590
Cdd:cd13981   8 LGEGGYASVYLAKDDDEQSDGSL--VALK----VEKPPSIWEFyicdqLHSRLKNSRLRE-SISGAHSAHLFQDESILVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMSGGDMKSFLR--HSRPHLGQPSPLVMRDLLQLAqDIAQGCHyleENHFIHRDIAARNCLL------------SCAGP 656
Cdd:cd13981  81 DYSSQGTLLDVVNkmKNKTGGGMDEPLAMFFTIELL-KVVEALH---EVGIIHGDIKPDNFLLrleicadwpgegENGWL 156
                       170
                ....*....|....*
gi 42544153 657 SRVAKIGDFGMARDI 671
Cdd:cd13981 157 SKGLKLIDFGRSIDM 171
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
512-731 2.97e-04

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: 43.90  E-value: 2.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIglpGDSSPLQVAIKTLPELCSPQDELDFLMEAL----IISKFRHQNIVRCVG-LSLRATPR 586
Cdd:cd14041  10 LLHLLGRGGFSEVYKAFDL---TEQRYVAVKIHQLNKNWRDEKKENYHKHACreyrIHKELDHPRIVKLYDyFSLDTDSF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 LILLELMSGGDMKSFLRhsrphlgQPSPLVMRDLLQLAQDIAQGCHYLEENH--FIHRDIAARNCLLSCAGPSRVAKIGD 664
Cdd:cd14041  87 CTVLEYCEGNDLDFYLK-------QHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITD 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 665 FGMARdIYRASYYRRGDRALLPVK------WMPPEAFLEG----IFTSKTDSWSFGVLLWEIFsLGYMPYPGRTNQE 731
Cdd:cd14041 160 FGLSK-IMDDDSYNSVDGMELTSQgagtywYLPPECFVVGkeppKISNKVDVWSVGVIFYQCL-YGRKPFGHNQSQQ 234
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
512-724 6.38e-04

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 42.32  E-value: 6.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIgLPGDSSPLQVAIKTLPELCspqdeldFLMEALIISKFRHQN-IVRCVGLSLRATPRLILL 590
Cdd:cd14130   4 VLKKIGGGGFGEIYEAMDL-LTRENVALKVESAQQPKQV-------LKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMsgGDMKSFLRHSRPHlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS-CAGPSRVAKIGDFGMAR 669
Cdd:cd14130  76 QLQ--GRNLADLRRSQPR----GTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrLPSTYRKCYMLDFGLAR 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42544153 670 DIYRASYYRRGDRALL----PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPY 724
Cdd:cd14130 150 QYTNTTGEVRPPRNVAgfrgTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPW 207
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
514-778 1.01e-03

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: 42.11  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 514 RALGHGAFGEVYEGLVIGlpgdsSPLQVAIKtlpELCSPQDELD--FLMEALIISKFR-HQNIVRCVGLSLRA------- 583
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVG-----TGKEYALK---RLLSNEEEKNkaIIQEINFMKKLSgHPNIVQFCSAASIGkeesdqg 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 584 -TPRLILLELMSGGDMKSFLRhsrphLGQPSPLVMRDLLQLaqdIAQGCHYLEENH-----FIHRDIAARNCLLSCAGps 657
Cdd:cd14036  78 qAEYLLLTELCKGQLVDFVKK-----VEAPGPFSPDTVLKI---FYQTCRAVQHMHkqsppIIHRDLKIENLLIGNQG-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 658 rVAKIGDFGMARDI-----YRASYYRRG------DRALLPVKWMPPEAFLEGIF--TSKTDSWSFGVLLweiFSLGYMPY 724
Cdd:cd14036 148 -QIKLCDFGSATTEahypdYSWSAQKRSlvedeiTRNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCIL---YLLCFRKH 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42544153 725 PGRTNQEVLdfVVGGGRMDPPRGCPGPVYR-IMTQCWQHEPELRPSFASILERLQ 778
Cdd:cd14036 224 PFEDGAKLR--IINAKYTIPPNDTQYTVFHdLIRSTLKVNPEERLSITEIVEQLQ 276
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
540-792 1.32e-03

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 41.78  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 540 QVAIK-TLPELCSpQDELDFLMEALIISK-FRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHlGQPSPLVM 617
Cdd:cd08226  27 LVTVKiTNLDNCS-EEHLKALQNEVVLSHfFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPE-GMNEALIG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 618 RDLLqlaqDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKI-GDFGMARDIYRASY---YRRGDRALLPvkWMPPE 693
Cdd:cd08226 105 NILY----GAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLsHLYSMVTNGQRSKVvydFPQFSTSVLP--WLSPE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 694 AFLEGI--FTSKTDSWSFGVLLWEIFSlGYMPYPG-RTNQEVLD--------------FVVGGGRMD------------- 743
Cdd:cd08226 179 LLRQDLhgYNVKSDIYSVGITACELAR-GQVPFQDmRRTQMLLQklkgppyspldifpFPELESRMKnsqsgmdsgiges 257
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 744 ------------------PPRGCPGPVYRIMTQCWQHEPELRPSFASILERL---QYCTQDPDVLNSLLP 792
Cdd:cd08226 258 vatssmtrtmtserlqtpSSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSffkQVKEQTQASLLSLLP 327
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
510-716 1.39e-03

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: 41.50  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 510 VTLLRALGHGAFGEVYegLVIGLP-GDSSPLQ-VAIKTLPELCSPQDELDFlMEALIiskfRHQNIVRCVGLSLRATPR- 586
Cdd:cd14037   5 VTIEKYLAEGGFAHVY--LVKTSNgGNRAALKrVYVNDEHDLNVCKREIEI-MKRLS----GHKNIVGYIDSSANRSGNg 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 587 ----LILLELMSGGDMKSFLrHSRPHLGQPSPLVMRDLLQLAQDIAQgCHYLEENhFIHRDIAARNCLLScagPSRVAKI 662
Cdd:cd14037  78 vyevLLLMEYCKGGGVIDLM-NQRLQTGLTESEILKIFCDVCEAVAA-MHYLKPP-LIHRDLKVENVLIS---DSGNYKL 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 663 GDFGMA-----------------RDIYR---ASYyrrgdRAllpvkwmpPEA---FLEGIFTSKTDSWSFGVLLWEI 716
Cdd:cd14037 152 CDFGSAttkilppqtkqgvtyveEDIKKyttLQY-----RA--------PEMidlYRGKPITEKSDIWALGCLLYKL 215
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
639-732 1.49e-03

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: 41.94  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 639 FIHRDIAARNCLLSCAGPsrvAKIGDFGMARDI----------------------YRASYYRRG----DRALLPVK---- 688
Cdd:cd05600 132 YIHRDLKPENFLIDSSGH---IKLTDFGLASGTlspkkiesmkirleevkntaflELTAKERRNiyraMRKEDQNYansv 208
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42544153 689 -----WMPPEAfLEGIFTSKT-DSWSFGVLLWEiFSLGYMPYPGRTNQEV 732
Cdd:cd05600 209 vgspdYMAPEV-LRGEGYDLTvDYWSLGCILFE-CLVGFPPFSGSTPNET 256
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
512-731 1.81e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 41.19  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYEGLVIgLPGDSSPLQVAIKTLPELCspqdeldFLMEALIISKFRHQN-IVRCVGLSLRATPRLILL 590
Cdd:cd14129   4 VLRKIGGGGFGEIYDALDL-LTRENVALKVESAQQPKQV-------LKMEVAVLKKLQGKDhVCRFIGCGRNDRFNYVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 591 ELMsgGDMKSFLRHSRPHlgqpSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLScAGPSRVAK--IGDFGMA 668
Cdd:cd14129  76 QLQ--GRNLADLRRSQSR----GTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMG-RFPSTCRKcyMLDFGLA 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 669 RDIYRASYYRRGDRALL----PVKWMPPEAFLEGIFTSKTDSWSFGVLLWEiFSLGYMPYPGRTNQE 731
Cdd:cd14129 149 RQFTNSCGDVRPPRAVAgfrgTVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKE 214
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
512-724 1.89e-03

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: 41.53  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 512 LLRALGHGAFGEVYeglvigLPGDSSPLQV-AIKTLPEL-CSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRL-I 588
Cdd:cd05622  77 VVKVIGRGAFGEVQ------LVRHKSTRKVyAMKLLSKFeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLyM 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSFLrhSRPHLGQPSPLVMRDLLQLAQDiaqGCHYLeenHFIHRDIAARNCLLSCAGPsrvAKIGDFGMA 668
Cdd:cd05622 151 VMEYMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALD---AIHSM---GFIHRDVKPDNMLLDKSGH---LKLADFGTC 219
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 669 RDIYRASYYrRGDRALLPVKWMPPEAFL----EGIFTSKTDSWSFGVLLWEIFsLGYMPY 724
Cdd:cd05622 220 MKMNKEGMV-RCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPF 277
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
516-724 2.09e-03

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: 40.88  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 516 LGHGAFGEVYeglviGLPGDSSPLQVAIKTLPE--LCSPQDELDFLMEALIISKFRHQN----IVrCVGLSLRATPRL-I 588
Cdd:cd05606   2 IGRGGFGEVY-----GCRKADTGKMYAMKCLDKkrIKMKQGETLALNERIMLSLVSTGGdcpfIV-CMTYAFQTPDKLcF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 589 LLELMSGGDMKSflrhsrpHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRvakIGDFGMA 668
Cdd:cd05606  76 ILDLMNGGDLHY-------HLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVR---ISDLGLA 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544153 669 RDIYR----ASYYRRGdrallpvkWMPPEAFLEGI-FTSKTDSWSFGVLLWEIFSlGYMPY 724
Cdd:cd05606 146 CDFSKkkphASVGTHG--------YMAPEVLQKGVaYDSSADWFSLGCMLYKLLK-GHSPF 197
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
623-726 2.76e-03

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 40.70  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 623 LAQDIAQGCHYLEENHFIHRDIAARNCLLsCAGPSRVAKIGDFGMA----RDIYraSY-----YRrgdrallpvkwmPPE 693
Cdd:cd14212 108 FLQQLLDALSVLKDARIIHCDLKPENILL-VNLDSPEIKLIDFGSAcfenYTLY--TYiqsrfYR------------SPE 172
                        90       100       110
                ....*....|....*....|....*....|...
gi 42544153 694 AFLEGIFTSKTDSWSFGVLLWEIFsLGYMPYPG 726
Cdd:cd14212 173 VLLGLPYSTAIDMWSLGCIAAELF-LGLPLFPG 204
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
639-734 2.90e-03

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: 40.76  E-value: 2.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 639 FIHRDIAARNCLLSCAGPsrvAKIGDFGMA---RDIYRASYYRRGDRALLPvKWMPPEAFLEGIFTSKTDSWSFGVLLWE 715
Cdd:cd05598 122 FIHRDIKPDNILIDRDGH---IKLTDFGLCtgfRWTHDSKYYLAHSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYE 197
                        90       100
                ....*....|....*....|...
gi 42544153 716 IFsLGYMPY----PGRTNQEVLD 734
Cdd:cd05598 198 ML-VGQPPFlaqtPAETQLKVIN 219
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
610-726 2.93e-03

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: 40.89  E-value: 2.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 610 GQPSPLVMRdllqLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMA----RDIY---RASYYRrgdr 682
Cdd:cd14224 164 GFSLQLVRK----FAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGI-KVIDFGSScyehQRIYtyiQSRFYR---- 234
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 42544153 683 allpvkwmPPEAFLEGIFTSKTDSWSFGVLLWEIFSlGYMPYPG 726
Cdd:cd14224 235 --------APEVILGARYGMPIDMWSFGCILAELLT-GYPLFPG 269
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
570-724 3.04e-03

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: 40.52  E-value: 3.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 570 HQNIVRCVGL---------SLRATPRLIL-LELMSGGDMksFLRHSRPHlGQPSPLVMRDLLQLAQDIaQGCHYLeenHF 639
Cdd:cd14171  58 HPNIVQIYDVyansvqfpgESSPRARLLIvMELMEGGEL--FDRISQHR-HFTEKQAAQYTKQIALAV-QHCHSL---NI 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 640 IHRDIAARNCLLSCAGPSRVAKIGDFGMAR----DIYRASY--YRRGDRALLPVKWMPPEafLEGIFTSKT--------D 705
Cdd:cd14171 131 AHRDLKPENLLLKDNSEDAPIKLCDFGFAKvdqgDLMTPQFtpYYVAPQVLEAQRRHRKE--RSGIPTSPTpytydkscD 208
                       170
                ....*....|....*....
gi 42544153 706 SWSFGVLLWeIFSLGYMPY 724
Cdd:cd14171 209 MWSLGVIIY-IMLCGYPPF 226
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
634-733 3.08e-03

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 40.67  E-value: 3.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 634 LEENHFIHRDIAARNCLLSCAgpSRVAKIGDFGMARDI-------YRAS-YYRrgdrallpvkwmPPEAFLEGIFTSKTD 705
Cdd:cd14135 121 LKKCNILHADIKPDNILVNEK--KNTLKLCDFGSASDIgeneitpYLVSrFYR------------APEIILGLPYDYPID 186
                        90       100
                ....*....|....*....|....*...
gi 42544153 706 SWSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14135 187 MWSVGCTLYELYT-GKILFPGKTNNHML 213
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
634-733 3.13e-03

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: 40.84  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 634 LEENHFIHRDIAARNCLLSCAGPSRVaKIGDFGMA----RDIY---RASYYRrgdrallpvkwmPPEAFLEGIFTSKTDS 706
Cdd:cd14225 162 LYRERIIHCDLKPENILLRQRGQSSI-KVIDFGSScyehQRVYtyiQSRFYR------------SPEVILGLPYSMAIDM 228
                        90       100
                ....*....|....*....|....*..
gi 42544153 707 WSFGVLLWEIFSlGYMPYPGRTNQEVL 733
Cdd:cd14225 229 WSLGCILAELYT-GYPLFPGENEVEQL 254
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
573-668 8.27e-03

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 39.06  E-value: 8.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 573 IVRCVGLSLRATPRLILLELMsGGDMKSFLRHSRPHLGQpsplvmRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLS 652
Cdd:cd14124  84 IPSCVGFGVHDSYRFLVFPSL-GQSLQSALDEGKGVLSE------KAVLQLACRLLDALEFIHENEYVHGDITAENIFVD 156
                        90
                ....*....|....*.
gi 42544153 653 CAGPSRVAKIGdFGMA 668
Cdd:cd14124 157 PEDQSEVYLAG-YGFA 171
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
569-714 8.36e-03

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: 38.98  E-value: 8.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544153 569 RHQNIVRCVGLSLRATPRLILLELMSGGDMksFLRHSrpHLGQPSPLVMRDLLQlaQDIAqGCHYLEENHFIHRDIAARN 648
Cdd:cd14662  54 RHPNIIRFKEVVLTPTHLAIVMEYAAGGEL--FERIC--NAGRFSEDEARYFFQ--QLIS-GVSYCHSMQICHRDLKLEN 126
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544153 649 CLLSCAGPSRVaKIGDFGMARDiyrASYYRRGDRALLPVKWMPPEAFLEGIFTSK-TDSWSFGVLLW 714
Cdd:cd14662 127 TLLDGSPAPRL-KICDFGYSKS---SVLHSQPKSTVGTPAYIAPEVLSRKEYDGKvADVWSCGVTLY 189
 
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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