Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  25 TVLERLGAD-----YLARDADGG-LVVLSVL--PWVRGPRSRAVAQARLEAAAQASSRHLARVVHSDVGGDKPHVVGEYV 96
Cdd:cd14014    3 RLVRLLGRGgmgevYRARDTLLGrPVAIKVLrpELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  97 DGPSLRDVVGADGPLPAAELAATARRTAAALAALHRAGTTHGAFEPGRVLY-PRGGAKVT--G-AGTADPDAREVAH--- 169
Cdd:cd14014   83 EGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLtEDGRVKLTdfGiARALGDSGLTQTGsvl 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 170 --PAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPF-GFGAGDVLARRITSRPPDLG----DLDGPLRDLLLRCLDK 242
Cdd:cd14014  163 gtPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHLQEAPPPPSplnpDVPPALDAIILRALAK 242

                        250
                 ....*....|....*...
gi 648622498 243 DPEARPTTSR-LVRVLRD 259
Cdd:cd14014  243 DPEERPQSAAeLLAALRA 260

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  25 TVLERLGAD-----YLARDADGG-LVVLSVL--PWVRGPRSRAVAQARLEAAAQASSRHLARVVHSDVGGDKPHVVGEYV 96
Cdd:cd14014    3 RLVRLLGRGgmgevYRARDTLLGrPVAIKVLrpELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  97 DGPSLRDVVGADGPLPAAELAATARRTAAALAALHRAGTTHGAFEPGRVLY-PRGGAKVT--G-AGTADPDAREVAH--- 169
Cdd:cd14014   83 EGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLtEDGRVKLTdfGiARALGDSGLTQTGsvl 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 170 --PAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPF-GFGAGDVLARRITSRPPDLG----DLDGPLRDLLLRCLDK 242
Cdd:cd14014  163 gtPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHLQEAPPPPSplnpDVPPALDAIILRALAK 242

                        250
                 ....*....|....*...
gi 648622498 243 DPEARPTTSR-LVRVLRD 259
Cdd:cd14014  243 DPEERPQSAAeLLAALRA 260

Protein kinase domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498   34 YLARDAD-GGLVVLSVLPwVRGPRSRAVAQARLEAAAQASSRH-----LARVVHSDvggDKPHVVGEYVDGPSLRDVVGA 107
Cdd:pfam00069  16 YKAKHRDtGKIVAIKKIK-KEKIKKKKDKNILREIKILKKLNHpnivrLYDAFEDK---DNLYLVLEYVEGGSLFDLLSE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  108 DGPLPAAELAatarrtaaalaalhragttHGAFEPGRVLYPrGGAKVTGAGTadpdarevahPAYQAPEHIEDEPVGAPA 187
Cdd:pfam00069  92 KGAFSEREAK-------------------FIMKQILEGLES-GSSLTTFVGT----------PWYMAPEVLGGNPYGPKV 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 648622498  188 DVWAWAATLVYAATGHPPFGFGAGDVLARRITSRPPDLGDLD 229
Cdd:pfam00069 142 DVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELP 183

Stk1 family PASTA domain-containing Ser/Thr kinase;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648622498  61 AQARLEAAAQASsrhlARVVHS------DVG--GDKPHVVGEYVDGPSLRDVVGADGPLPAAE 115
Cdd:NF033483  50 FVARFRREAQSA----ASLSHPnivsvyDVGedGGIPYIVMEYVDGRTLKDYIREHGPLSPEE 108

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  25 TVLERLGAD-----YLARDADGG-LVVLSVL--PWVRGPRSRAVAQARLEAAAQASSRHLARVVHSDVGGDKPHVVGEYV 96
Cdd:cd14014    3 RLVRLLGRGgmgevYRARDTLLGrPVAIKVLrpELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  97 DGPSLRDVVGADGPLPAAELAATARRTAAALAALHRAGTTHGAFEPGRVLY-PRGGAKVT--G-AGTADPDAREVAH--- 169
Cdd:cd14014   83 EGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLtEDGRVKLTdfGiARALGDSGLTQTGsvl 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 170 --PAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPF-GFGAGDVLARRITSRPPDLG----DLDGPLRDLLLRCLDK 242
Cdd:cd14014  163 gtPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHLQEAPPPPSplnpDVPPALDAIILRALAK 242

                        250
                 ....*....|....*...
gi 648622498 243 DPEARPTTSR-LVRVLRD 259
Cdd:cd14014  243 DPEERPQSAAeLLAALRA 260

Protein kinase domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498   34 YLARDAD-GGLVVLSVLPwVRGPRSRAVAQARLEAAAQASSRH-----LARVVHSDvggDKPHVVGEYVDGPSLRDVVGA 107
Cdd:pfam00069  16 YKAKHRDtGKIVAIKKIK-KEKIKKKKDKNILREIKILKKLNHpnivrLYDAFEDK---DNLYLVLEYVEGGSLFDLLSE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  108 DGPLPAAELAatarrtaaalaalhragttHGAFEPGRVLYPrGGAKVTGAGTadpdarevahPAYQAPEHIEDEPVGAPA 187
Cdd:pfam00069  92 KGAFSEREAK-------------------FIMKQILEGLES-GSSLTTFVGT----------PWYMAPEVLGGNPYGPKV 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 648622498  188 DVWAWAATLVYAATGHPPFGFGAGDVLARRITSRPPDLGDLD 229
Cdd:pfam00069 142 DVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELP 183

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.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 648622498 170 PAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPF 206
Cdd:cd05122  161 PYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY 197

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.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 648622498 172 YQAPEHIEDEP--VGAPADVWAWAATLVYAATGHPPF 206
Cdd:cd06624  175 YMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPF 211

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.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 648622498 170 PAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPF 206
Cdd:cd06606  165 PYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW 201

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 167 VAHPAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPFGFGAGDVLARRI---------TSRPPDLGDLdgplrdlLL 237
Cdd:cd08529  162 VGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIvrgkyppisASYSQDLSQL-------ID 234

                         90
                 ....*....|....*...
gi 648622498 238 RCLDKDPEARPTTSRLVR 255
Cdd:cd08529  235 SCLTKDYRQRPDTTELLR 252

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 160 ADPDAREVAHPAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPFgFGAGD------VLARRITSRPPDLGDLDGPLR 233
Cdd:cd14107  153 SEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPF-AGENDratllnVAEGVVSWDTPEITHLSEDAK 231

                         90
                 ....*....|....*...
gi 648622498 234 DLLLRCLDKDPEARPTTS 251
Cdd:cd14107  232 DFIKRVLQPDPEKRPSAS 249

Stk1 family PASTA domain-containing Ser/Thr kinase;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648622498  61 AQARLEAAAQASsrhlARVVHS------DVG--GDKPHVVGEYVDGPSLRDVVGADGPLPAAE 115
Cdd:NF033483  50 FVARFRREAQSA----ASLSHPnivsvyDVGedGGIPYIVMEYVDGRTLKDYIREHGPLSPEE 108

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648622498 170 PAYQAPEHIEDEPVGA---PADVWAWAATLVYAATGHPPFGFGAGD--VLARRITSRPPDL 225
Cdd:cd06618  178 AAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfeVLTKILNEEPPSL 238

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  91 VVGEYVDGPSLRDVVGADGPLPAAELAATARRTAAALAALHRAGTTHGAFEPGRVLY----PR-------GGAKVTGAGT 159
Cdd:cd14098   78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqddPVivkisdfGLAKVIHTGT 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 160 ADPDAreVAHPAYQAPEHIEDEPVGAP------ADVWAWAATLVYAATGHPPFGFGAGDVLARRITS----RPPDLG-DL 228
Cdd:cd14098  158 FLVTF--CGTMAYLAPEILMSKEQNLQggysnlVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKgrytQPPLVDfNI 235

                        170       180
                 ....*....|....*....|....*..
gi 648622498 229 DGPLRDLLLRCLDKDPEARPTTSRLVR 255
Cdd:cd14098  236 SEEAIDFILRLLDVDPEKRMTAAQALD 262

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 648622498 169 HPAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPFGFGAGDVLARRITSRPP 223
Cdd:cd14010  173 TPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDP 227

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 170 PAYQAPEHIEDEPVGAPADVWAwAATLVYAA-TGHPPFgFGAGD------VLARRITSRPPDLGDLDGPLRDLLLRCLDK 242
Cdd:cd14006  154 PEFVAPEIVNGEPVSLATDMWS-IGVLTYVLlSGLSPF-LGEDDqetlanISACRVDFSEEYFSSVSQEAKDFIRKLLVK 231

                 ....*....
gi 648622498 243 DPEARPTTS 251
Cdd:cd14006  232 EPRKRPTAQ 240

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498  62 QARLEAAAQASSRHLARVVHSDVGGDKPHVVGEYVDGPSLRDVVgADGPLPAAELAATARRTAAALAALHRAGTTHGAFE 141
Cdd:cd06641   50 QQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLL-EPGPLDETQIATILREILKGLDYLHSEKKIHRDIK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648622498 142 PGRVLYPRGG-AKVTGAGTA----DPDARE---VAHPAYQAPEHIEDEPVGAPADVWAWAATLVYAATGHPPFG-FGAGD 212
Cdd:cd06641  129 AANVLLSEHGeVKLADFGVAgqltDTQIKRn*fVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSeLHPMK 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648622498 213 VLARRITSRPPDL-GDLDGPLRDLLLRCLDKDPEARPTTSRLVR---VLRDEAPHEERTgpRRIPRY-RWR 278
Cdd:cd06641  209 VLFLIPKNNPPTLeGNYSKPLKEFVEACLNKEPSFRPTAKELLKhkfILRNAKKTSYLT--ELIDRYkRWK 277